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			<p class="title- ParaOverride-1" xml:lang="en-GB">Biology, Expression, and Regulation of Host Defense Peptides: A Minireview</p>
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			<p class="Authors ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Authors ParaOverride-1" xml:lang="en-GB"><span class="CharOverride-2">Lakshmi Tulasi Sunkara</span><span class="CharOverride-3">1</span><span class="CharOverride-2">, Amanda Renee Curtis</span><span class="CharOverride-3">1</span><span class="CharOverride-2">,</span><span class="CharOverride-3"> </span><span class="CharOverride-2">Guolong Zhang</span><span class="CharOverride-3">1, 2, 3*</span></p>
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			<p class="Affiliations ParaOverride-1" xml:lang="en-GB"><span class="CharOverride-4">1</span>Department of Animal Science; <span class="CharOverride-4">2</span>Department of Biochemistry and Molecular Biology; <span class="CharOverride-4">3</span>Department of Physiological Sciences, Center for Veterinary Health Sciences, Oklahoma State University, Stillwater, OK 74078, USA.</p>
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			<p class="Abstract ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Abstract ParaOverride-1" xml:lang="en-GB"><span class="CharOverride-5">Abstract</span> | Host defence peptides (HDPs) represent a diverse group of small peptides generally consisting of less than 100 amino acid residues with a net positive charge. HDPs are synthesized preferably by phagocytes in the circulation, skin keratinocytes, and mucosal epithelial cells of the digestive, respiratory, and urogenital tracts. As important effector molecules of innate immunity, HDPs are quickly mobilized to fight off infections. In addition to direct antimicrobial activities, HDPs impact positively on wound healing, inflammation resolution, and development of adaptive immunity. Besides infection and inflammation, many HDPs were found recently to be induced by a large number of dietary compounds such as vitamins D, short-chain fatty acids, histone deacetylase inhibitors, zinc, and certain phytochemicals in humans and several other animal species such as poultry. Further investigations on the dietary modulation of HDP synthesis may lead to the development of a novel antibiotic-free approach to disease control and prevention with applications in both the livestock and poultry industry and human health.</p>
		  <p class="Abstract ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Abstract ParaOverride-1" xml:lang="en-GB"><span class="CharOverride-5">Keywords </span>| Host defence peptides, Antimicrobial resistance, Immune modulation, Antibiotic alternatives, Innate immunity</p>
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			<p class="Editor----Citation" xml:lang="en-GB"><span class="CharOverride-6">Editor</span> | Muhammad Munir (DVM, PhD), Avian Viral Diseases Program, Compton Laboratory, Newbury, Berkshire, RG20 7NN, UK.</p>
			<p class="Editor----Citation" xml:lang="en-GB"><span class="CharOverride-6">Special Issue</span> | 3(2015) “Poultry diseases and the strategies for their control and prevention”</p>
			<p class="Editor----Citation" xml:lang="en-GB"><span class="CharOverride-5">Received</span> | June 04, 2015; <span class="CharOverride-5">Revised</span> | June 20, 2015; <span class="CharOverride-5">Accepted</span> | June 21, 2015; <span class="CharOverride-5">Published</span> | June 29, 2015&#9;&#9;</p>
			<p class="Editor----Citation" xml:lang="en-GB"><span class="CharOverride-5">*Correspondence</span> | Guolong Zhang, Oklahoma State University, Stillwater, USA; <span class="CharOverride-5">Email:</span> zguolon@okstate.edu</p>
			<p class="Editor----Citation" xml:lang="en-GB"><span class="CharOverride-5">Citation</span> | Sunkara LT, Curtis AR, Zhang G (2015). Biology, expression, and regulation of host defense peptides: A minireview. Adv. Anim. Vet. Sci. 3(3s): 9-20.  </p>
			<p class="Editor----Citation" xml:lang="en-GB"><span class="CharOverride-6">DOI</span> | ><a href="http://dx.doi.org/10.14737/journal.aavs/2015/3.3s.9.20"><span class="Hyperlink">http://dx.doi.org/10.14737/journal.aavs/2015/3.3s.9.20</span></a></p>
			<p class="Editor----Citation" xml:lang="en-GB"><span class="Editor---Citation CharOverride-5" xml:lang="en-US">ISSN </span><span class="Editor---Citation CharOverride-5" xml:lang="en-US">(</span><span class="Editor---Citation CharOverride-5" xml:lang="en-US">Online</span><span class="Editor---Citation CharOverride-5" xml:lang="en-US">)</span> | 2307-8316; <span class="Editor---Citation CharOverride-5" xml:lang="en-US">ISSN </span><span class="Editor---Citation CharOverride-5" xml:lang="en-US">(Print) </span>| 2309-3331</p>
			<p class="Editor----Citation" xml:lang="en-GB"><span class="CharOverride-6">Copyright </span>© 2015 Sunkara et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</p>
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			<p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">INTRODUCTION</p>
			<p class="Caps-on-First-Para ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Caps-on-First-Para ParaOverride-1" xml:lang="en-GB"><span class="_idGenDropcap-1">I</span><span>nnate </span>immunity is the first line of host defense and crucial to protect all living organisms against microbial invasions (<a href="#Linde-A--Ross-CR--Dav"><span class="Hyperlink">Linde et al., 2008</span></a>; <a href="#Steinstraesser-L--Koehler-T--Jacobsen"><span class="Hyperlink">Steinstraesser et al., 2011</span></a>). As critical effector molecules of the innate immune system, host defense peptides (HDPs), also known as antimicrobial peptides, have been discovered in nearly all forms of life (<a href="#Zasloff-M--2002"><span class="Hyperlink">Zasloff, 2002</span></a>; <a href="#Zhang-G--Sunkara-LT--2014"><span class="Hyperlink">Zhang and Sunkara, 2014</span></a>). HDPs are strategically expressed in leukocytes as well as mucosal epithelial cells lining the respiratory, gastrointestinal and urogenital systems of their host (<a href="#Zhang-G--Sunkara-LT--2014"><span class="Hyperlink">Zhang and Sunkara, 2014</span></a>). They are synthesized as peptide precursors and enzymatically processed to release biologically active, mature peptides (<a href="#Steinstraesser-L--Koehler-T--Jacobsen"><span class="Hyperlink">Steinstraesser et al., 2011</span></a>; <a href="#Zasloff-M--2002"><span class="Hyperlink">Zasloff, 2002</span></a>). Most mature HDPs consist of 12 to100 amino acids rich in cationic residues and are largely amphipathic (<a href="#Wang-G--2014-"><span class="Hyperlink">Wang, 2014</span></a>). They directly kill a myriad of microbes ranging from Gram-positive and Gram-negative bacteria to fungi, protozoa, parasites, enveloped viruses, and even cancerous cells. Additionally, many HDPs have a profound impact on the regulation of inflammation, wound healing, and adaptive immunity (<a href="#Hilchie-AL--Wuerth"><span class="Hyperlink">Hilchie et al., 2013</span></a>; <a href="#Yeung-ATY--Gellatly-SL--Hancock-REW--2011"><span class="Hyperlink">Yeung et al., 2011</span></a>). Because of these pleotropic activities, these HDPs are being actively explored as novel antimicrobials for disease control and prevention particularly against drug-resistant microbes (<a href="#Hancock-RE--Nijnik-A--Philpott-DJ--2012-"><span class="Hyperlink">Hancock et al., 2012</span></a>). </p>
		  <p class="Caps-on-First-Para ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">CLASSIFICATION OF HDPs</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Nearly 2,500 HDPs have been reported in bacteria, protozoa, fungi, plants, and animals (<a href="#Fjell-CD--Hancock-RE--Cherkasov-A--2007-."><span class="Hyperlink">Fjell et al., 2007</span></a>; <a href="#Wang-G--Li-X--Wang-Z--2009-"><span class="Hyperlink">Wang et al., 2009</span></a>). Based on their structures, HDPs are broadly classified into four major groups including the peptides adopting largely an <span class="CharOverride-10">α</span>-helical, <span class="CharOverride-10">β</span>-sheet, a loop or flexible structure (<a href="#Pasupuleti-M--Schmidtchen-A--Malm"><span class="Hyperlink">Pasupuleti et al., 2012</span></a>; <a href="#Yeung-ATY--Gellatly-SL--Hancock-REW--2011"><span class="Hyperlink">Yeung et al., 2011</span></a>). The loop structure of HDPs is mainly due to the presence of a disulfide bond, whereas flexible structures result from enrichment of certain amino acids such as arginine, histidine, proline, and tryptophan. Cathelicidins and defensins represent two major families of HDPs found in vertebrates (<a href="#Sang-Y--Blecha-F--2009"><span class="Hyperlink">Sang and Blecha, 2009</span></a>; <a href="#Sorensen-OE--Borregaard-N"><span class="Hyperlink">Sorensen et al., 2008</span></a>; <a href="#van-Dijk-A--Molhoek-EM-2011"><span class="Hyperlink">van Dijk et al., 2011</span></a>). Cathelicidins were first isolated from bovine neutrophils as cyclic dodecapeptides (<a href="#Romeo-D--Skerlavaj-B--Bolog"><span class="Hyperlink">Romeo et al., 1988</span></a>). Since then, cathelicidins have been found in not only mammals but also in fish, snakes, and birds (<a href="#Chang-CI--Zhang-YA-"><span class="Hyperlink">Chang et al., 2006</span></a>; <a href="#Gennaro-R--Zanetti-M--20"><span class="Hyperlink">Gennaro and Zanetti, 2000</span></a>; <a href="#Lynn-DJ--Higgs-R--Gaines-S--T"><span class="Hyperlink">Lynn et al., 2004</span></a>; <a href="#Uzzell-T--Stolzenberg-ED--Shinn"><span class="Hyperlink">Uzzell et al., 2003</span></a>; <a href="#van-Dijk-A--Veldhuizen-2005"><span class="Hyperlink">van Dijk et al., 2005</span></a>; <a href="#Xiao-Y--Cai-Y--Bommine"><span class="Hyperlink">Xiao et al., 2006</span></a>; <a href="#Zhao-H--Gan-TX--Li-2008"><span class="Hyperlink">Zhao et al., 2008</span></a>). The name cathelicidin was coined from the presence of a highly conserved cathelin domain in the N-terminal region. The C-terminal regions of cathelicidins are highly variable among species and possess different biological functions (<a href="#Gennaro-R--Zanetti-M--20"><span class="Hyperlink">Gennaro and Zanetti, 2000</span></a>; <a href="#Kolls-JK--McCray-PB--Jr.--Chan-YR--2008"><span class="Hyperlink">Kolls et al., 2008</span></a>). A large group of cathelicidin genes are encoded in the porcine, ovine, and bovine genomes; however, only a single cathelicidin gene exists in rodents, dogs, primates, and humans (<a href="#Steinstraesser-L--Koehler-T--Jacobsen"><span class="Hyperlink">Steinstraesser et al., 2011</span></a>; <a href="#van-Dijk-A--Molhoek-EM-2011"><span class="Hyperlink">van Dijk et al., 2011</span></a>). Four cathelicidin genes were found recently in chickens (<a href="#Goitsuka-R--Chen-CL--Benyon-L--Asano-Y--Kitamura-D--Cooper-MD--2007-.-Chicken"><span class="Hyperlink">Goitsuka et al., 2007</span></a>; <a href="#Xiao-Y--Cai-Y--Bommine"><span class="Hyperlink">Xiao et al., 2006</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Defensins, present in plants, invertebrates and vertebrates, are rich in cysteines and comprised of 3-4 disulfide bonds (<a href="#Carvalho-Ade-O--Gomes-VM--2009"><span class="Hyperlink">Carvalho-Ade and Gomes, 2009</span></a>; <a href="#Strominger-JL--2009"><span class="Hyperlink">Strominger, 2009</span></a>; <a href="#van-Dijk-A--Veldh-2008"><span class="Hyperlink">van Dijk et al., 2008</span></a>). Most vertebrate defensins consist of a signal peptide, proregion and cationic mature peptide with six conserved cysteine residues forming three intramolecular disulfide bridges creating a “defensin-like” fold (<a href="#Hiemstra-PS--2007"><span class="Hyperlink">Hiemstra, 2007</span></a>; <a href="#Lehrer-RI--Ganz-T--2002"><span class="Hyperlink">Lehrer and Ganz, 2002</span></a>). Based on the spacing pattern and pairing of cysteine residues, vertebrate defensins are classified into three major subfamilies namely <span class="CharOverride-10">α</span>-, <span class="CharOverride-10">β</span>-, and <span class="CharOverride-10">θ</span>- defensins (<a href="#Hiemstra-PS--2007"><span class="Hyperlink">Hiemstra, 2007</span></a>). The disulfide bridges are formed between C1-C6, C2-C4, and C3-C5 in <span class="CharOverride-10">α</span>-defensins, whereas C1-C5, C2-C4, and C3-C6 are paired in <span class="CharOverride-10">β</span>-defensins, and C1-C6, C2-C5 and C3-C4 paired in <span class="CharOverride-10">θ</span>-defensins. Triple-stranded, anti-parallel <span class="CharOverride-10">β</span>-sheet structures are present in <span class="CharOverride-10">α</span>- and <span class="CharOverride-10">β</span>-defensins, while <span class="CharOverride-10">θ</span>-defensins are composed of circular double-stranded <span class="CharOverride-10">β</span>-sheets (<a href="#Selsted-ME--2004"><span class="Hyperlink">Selsted, 2004</span></a>; <a href="#Selsted-ME--Ouellette-AJ--2005"><span class="Hyperlink">Selsted and Ouellette, 2005</span></a>; <a href="#Steinstraesser-L--Koehler-T--Jacobsen"><span class="Hyperlink">Steinstraesser et al., 2011</span></a>; <a href="#van-Dijk-A--Veldh-2008"><span class="Hyperlink">van Dijk et al., 2008</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">As important effector molecules of innate immunity, cathelicidins and defensins are produced strategically by leukocytes, skin keratinocytes, and mucosal epithelial cells of respiratory, gastrointestinal, and urogenital tracts (<a href="#Brown-KL--Hancock-RE--"><span class="Hyperlink">Brown and Hancock, 2006</span></a>; <a href="#Hancock-RE--Scott-MG--2000"><span class="Hyperlink">Hancock and Scott, 2000</span></a>). In humans, cathelicidin LL-37 is mainly found in both leukocytes and epithelial cells, while <span class="CharOverride-10">α</span>- and <span class="CharOverride-10">θ</span>-defensins are commonly expressed in neutrophils and paneth cells of the small intestine, and the primary source of <span class="CharOverride-10">β</span>-defensins are mucosal epithelia and skin (<a href="#Easton-DM--Nijnik-A--Mayer-ML--Hancock-RE--2009-.-Potential-of-immunomodulatory-host-defense-pep"><span class="Hyperlink">Easton et al., 2009</span></a>; <a href="#Lehrer-RI--2004"><span class="Hyperlink">Lehrer, 2004</span></a>). HDP precursors are processed post translationally by different proteolytic enzymes to become biologically active (<a href="#Auvynet-C--Rosenstein-Y--2009-"><span class="Hyperlink">Auvynet and Rosenstein, 2009</span></a>; <a href="#Zanetti-M--Gennaro-R--Romeo-D--1995"><span class="Hyperlink">Zanetti et al., 1995</span></a>). For example, human <span class="CharOverride-10">α</span>-defensin HD5 is synthesized by intestinal Paneth cells and processed by trypsin (<a href="#Oppenheim-JJ--Biragyn-A--Kwa"><span class="Hyperlink">Oppenheim, 2003</span></a>). Human cathelicidin LL-37 is further processed by serine proteases like proteinase 3 in neutrophils and kallikreins 5 and 7 in the skin (<a href="#Guani-Guerra-E--Santos-Mendoza-T--Lugo-Reyes-SO--Teran-LM--20"><span class="Hyperlink">Guani-Guerra et al., 2010</span></a>; <a href="#Sorensen-OE--Follin-2001"><span class="Hyperlink">Sorensen et al., 2001</span></a>), whereas elastase is a main enzyme responsible for cleavage of cathelicidin precursors in cattle and pigs (<a href="#Panyutich-AV--Panyutich-E-1993"><span class="Hyperlink">Panyutich et al., 1997</span></a>; <a href="#Scocchi-M--Skerlavaj-B--Romeo-D--Gennaro-R--1992"><span class="Hyperlink">Scocchi et al., 1992</span></a>; <a href="#Zanetti-M--Litteri-1991"><span class="Hyperlink">Zanetti et al., 1991</span></a>).</p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction---- ParaOverride-1" xml:lang="en-GB">ANTIMICROBIAL PROPERTIES OF HDPs</p>
		  <p class="Heading-1--Introduction---- ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">HDPs are broad-spectrum natural antibiotics that kill or suppress the growth of a wide range of bacteria, mycobacteria, fungi, parasites, and certain enveloped viruses (<a href="#Bernard-JJ--Gallo-RL--2011"><span class="Hyperlink">Bernard and Gallo, 2011</span></a>). They kill microbes by physical disruption of membranes or by nonspecific inhibition of cellular transcription and translation (<a href="#Yeung-ATY--Gellatly-SL--Hancock-REW--2011"><span class="Hyperlink">Yeung et al., 2011</span></a>). Cationic HDPs initially accumulate and electrostatically interact with anionic membrane components such as lipopolysaccharides (LPS) of Gram-negative bacteria and lipoteichoic acid (LTA) of Gram-positive bacteria. Penetration into negatively charged phospholipids of microbial membranes resulting in membrane perturbation and leakage of intracellular contents, ultimately leading to cell death (<a href="#Hale-JD--Hancock-RE--200"><span class="Hyperlink">Hale and Hancock, 2007</span></a>; <a href="#Zasloff-M--2002"><span class="Hyperlink">Zasloff, 2002</span></a>). Because it is very difficult for microbes to change the overall negative charge of their membrane phospholipids, development of resistance against HDPs is extremely rare (<a href="#Yeaman-MR--Yount-NY--2003"><span class="Hyperlink">Yeaman and Yount, 2003</span></a>). Preferred disruption of microbial, but not host, membranes is believed to be due to the differences between prokaryotic and eukaryotic cell membrane properties. While the former is heavily negatively charged with high transmembrane potential (-140 mV), the latter is largely uncharged with a high cholesterol content and low transmembrane potential of approximately -15 mV (<a href="#Huang-Y--Huang-J--Chen-Y--"><span class="Hyperlink">Huang et al., 2010</span></a>; <a href="#Yount-NY--Yeaman-MR--2005"><span class="Hyperlink">Yount and Yeaman, 2005</span></a>). The mechanism of pore formation on microbial membranes varies among individual HDPs. Depending upon the net charge and spatial structure, HDPs permeate membranes via “barrel-stave”, “toroidal-pore”, “molecular electroporation”, “sinking raft”, or “carpet-wormhole” mechanisms (<a href="#Oren-Z--Shai-Y--1998"><span class="Hyperlink">Oren and Shai, 1998</span></a>; <a href="#Palffy-R--Gardlik-R--Behuliak-M--Kadasi-L--Turna-J--Celec-P--2009"><span class="Hyperlink">Palffy et al., 2009</span></a>; <a href="#van-Dijk-A--Veldh-2008"><span class="Hyperlink">van Dijk et al., 2008</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">In addition to direct disruption of membranes, certain HDPs, particularly <span class="CharOverride-10">α</span>- and <span class="CharOverride-10">θ</span>-defensins, suppress viral proliferation by acting as collectins. For example, retrocyclins (primate <span class="CharOverride-10">θ</span>-defensins) bind to glycoproteins (gp41 and gp120) of HIV as well as CD4 of host immune cells and prevent viral entry by blocking the conformational change of gp41, which is required for attachment and fusion of viruses with host cells (<a href="#Penberthy-WT--Chari-S--Cole-AL--Cole"><span class="Hyperlink">Penberthy et al., 2011</span></a>). Similarly, human <span class="CharOverride-10">α</span>-defensins (HNP1, -2, and -3) bind to envelop glycoprotein B of herpes simplex virus to suppress viral entry into the host cells (<a href="#Hazrati-E--Galen-B--Lu-W"><span class="Hyperlink">Hazrati et al., 2006</span></a>). Because of these diverse interactions with microbes, it is extremely difficult for microbes to develop resistance against HDPs.</p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp; </p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">ANTIINFLAMMATORY EFFECTS OF HDPs</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Besides antimicrobial properties, HDPs suppress inflammation and protect the host from excessive production of proinflammatory mediators triggered by microbial products. HDPs are capable of neutralizing bacterial endotoxins, inhibiting proinflammatory cytokine production, inducing antiinflammatory cytokines, and preventing activation of classical and lectin complement cascades (<a href="#Choi-KY--Chow-LN--Mookh"><span class="Hyperlink">Choi et al., 2012</span></a>; <a href="#Easton-DM--Nijnik-A--Mayer-ML--Hancock-RE--2009-.-Potential-of-immunomodulatory-host-defense-pep"><span class="Hyperlink">Easton et al., 2009</span></a>; <a href="#Groeneveld-TW--Ramwadhdoebe-TH-"><span class="Hyperlink">Groeneveld et al., 2007</span></a>). For example, human cathelicidin LL-37 binds to and neutralizes LPS and LTA, thereby abolishing the production of proinflammatory cytokines such as TNF-<span class="CharOverride-10">α</span>, IL-1<span class="CharOverride-10">β</span>, and IL-6, while also stimulating the expression of antiinflammatory cytokines such as IL-10 (<a href="#Mookherjee-N--Brown-KL"><span class="Hyperlink">Mookherjee et al., 2006</span></a>; <a href="#Mookherjee-N--Hancock-RE--2007"><span class="Hyperlink">Mookherjee and Hancock, 2007</span></a>; <a href="#Ruan-Y--Shen-T--Wang-Y--Hou-M--Li-J-"><span class="Hyperlink">Ruan et al., 2013</span></a>; <a href="#Scott-A--Weldon-S--Buchanan"><span class="Hyperlink">Scott et al., 2011</span></a>; <a href="#Suphasiriroj-W--Mikami"><span class="Hyperlink">Suphasiriroj et al., 2013</span></a>). In addition, LL-37 inhibits IFN-<span class="CharOverride-10">γ</span>-induced cell activation, proliferation, and production of proinflammatory and Th1-polarizing cytokines and antibodies in antigen- presenting cells (<a href="#Nijnik-A--Pistolic-J--Wyatt"><span class="Hyperlink">Nijnik et al., 2009</span></a>). In a murine infection model, LL-37 protects mice from septic shock induced by <span class="CharOverride-12">Pseudomonas aeruginosa</span> (<a href="#Kirikae-T--Hirata-M--Yamasu-H--Kiri"><span class="Hyperlink">Kirikae et al., 1998</span></a>). It also promotes secondary necrosis of apoptotic neutrophils without causing loss of membrane integrity or provoking inflammatory response of macrophages (<a href="#Li-HN--Barlow-PG-2009b"><span class="Hyperlink">Li et al., 2009b</span></a>). Likewise, chicken cathelicidin fowlicidin-1 prevents LPS-induced production of nitric oxide and TNF-<span class="CharOverride-10">α</span> (<a href="#Bommineni-YR--Acha"><span class="Hyperlink">Bommineni et al., 2010</span></a>). Porcine cathelicidin PR-39 inhibits the production of reactive oxygen species, while bovine cathelicidin BAMP-28 induces apoptosis of activated lymphocytes (<a href="#Brown-KL--Hancock-RE--"><span class="Hyperlink">Brown and Hancock, 2006</span></a>).</p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Similar to cathelicidins, defensins also inhibit production of proinflammatory cytokines by binding to microbial membranes, surface adhesins, and bacterial toxins as well as by surpressing their attachment to host cells (<a href="#Kohlgraf-KG--Pingel-LC--Dietrich-D"><span class="Hyperlink">Kohlgraf et al., 2010</span></a>). For example, human <span class="CharOverride-10">α</span>-defensin HNP1 attenuates LPS-mediated production of proinflammatory cytokines such as IL-1<span class="CharOverride-10">β</span> from monocytes (<a href="#Shi-J--Aono-S--Lu-W--Ouellette-AJ"><span class="Hyperlink">Shi et al., 2007</span></a>). HNP2 and HNP3 reduce production of several proinflammatory cytokines including IL-1 <span class="CharOverride-10">β</span>, IL-6, IL-8 and TNF-<span class="CharOverride-10">α</span> from LPS-stimulated human monocyte-derived macrophages (<a href="#Miles-K--Clarke-DJ--Lu-W--Sibinsk"><span class="Hyperlink">Miles et al., 2009</span></a>). Human <span class="CharOverride-10">β </span>defensin(HBD)-3 also abrogates the induction of IL-6, and TNF-<span class="CharOverride-10">α</span> from human myeloid dendritic cells stimulated with <span class="CharOverride-12">Porphyromonas gingivalis</span> (<a href="#Pingel-LC--Kohlgraf-KG--Han"><span class="Hyperlink">Pingel et al., 2008</span></a>). Moreover, there is evidence that expression of human <span class="CharOverride-10">α</span>- and <span class="CharOverride-10">β</span>-defensins is reduced in inflammatory diseases like Crohn’s disease, emphasizing the role of defensins in regulation of inflammation (<a href="#Guani-Guerra-E--Santos-Mendoza-T--Lugo-Reyes-SO--Teran-LM--20"><span class="Hyperlink">Guani-Guerra et al., 2010</span></a>; <a href="#Salzman-NH--2010"><span class="Hyperlink">Salzman, 2010</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">IMMUNOMODULATORY ACTIVITIES OF HDPs</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">HDPs have the capacity to directly kill pathogens, but their antimicrobial activity is often diminished in biological fluids in the presence of monovalent and divalent cations, serum, and polyanionic molecules like glycosaminoglycans (<a href="#Bowdish-DM--Davidso"><span class="Hyperlink">Bowdish et al., 2005</span></a>). Several HDPs, albeit with extremely weak or no antibacterial activities, have been found to still protect the host from infections, implying a host defense role other than directly killing bacteria (<a href="#Brown-KL--Hancock-RE--"><span class="Hyperlink">Brown and Hancock, 2006</span></a>; <a href="#Jenssen-H--Hancock-RE--2010"><span class="Hyperlink">Jenssen and Hancock, 2010</span></a>; <a href="#Yeung-ATY--Gellatly-SL--Hancock-REW--2011"><span class="Hyperlink">Yeung et al., 2011</span></a>). In fact, HDPs promote diverse immunomodulatory functions by stimulating the production of chemokines and cytokines, and by regulating complement activation, promoting wound healing, and by acting as chemoattractants (<a href="#Pundir-P--Kulka-M--2010"><span class="Hyperlink">Pundir and Kulka, 2010</span></a>; <a href="#van-Dijk-A--Molhoek-EM-2011"><span class="Hyperlink">van Dijk et al., 2011</span></a>; <a href="#Yeung-ATY--Gellatly-SL--Hancock-REW--2011"><span class="Hyperlink">Yeung et al., 2011</span></a>). For example, Human <span class="CharOverride-10">β</span>-defensins (HBD1 and HBD3) chemoattract immature dendritic cells and memory T cells, while human <span class="CharOverride-10">α</span>-defensins are chemotactic to naïve T cells (<a href="#Auvynet-C--Rosenstein-Y--2009-"><span class="Hyperlink">Auvynet and Rosenstein, 2009</span></a>). Similarly, HNP1-3 and HBD3-4 stimulate migration of neutrophils and monocytes, whereas LL-37 and HNP1-3 are chemotactic to mast cells and induce degranulation to release histamine and prostaglandin-2, respectively (<a href="#Auvynet-C--Rosenstein-Y--2009-"><span class="Hyperlink">Auvynet and Rosenstein, 2009</span></a>). HDPs also induce production of various pro-inflammatory cytokines such as IL-1<span class="CharOverride-10">β</span>, TNF-<span class="CharOverride-10">α</span> and IL-6 as well as chemokines such as IL-8 and monocyte chemotactic protein-1 from mononuclear phagocytes and epithelial cells (<a href="#Auvynet-C--Rosenstein-Y--2009-"><span class="Hyperlink">Auvynet and Rosenstein, 2009</span></a>; <a href="#van-Dijk-A--Tersteeg-2009"><span class="Hyperlink">van Dijk et al., 2009</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">In addition to modulation of host immunity, HDPs enhance wound healing. HDPs promote re-epithelialization, angiogenesis and vascularization by inducing proliferation of epithelial cells and vascular endothelial cells and chemoattracting fibroblasts and macrophages (<a href="#Steinstraesser-L--Koehler-T--Jacobsen"><span class="Hyperlink">Steinstraesser et al., 2011</span></a>). LL-37 was shown to enhance the closure of wounds in human corneal epithelial cells and in high-glucose-attenuated porcine corneal epithelial cells (<a href="#Yin-J--Yu-FS--2010"><span class="Hyperlink">Yin and Yu, 2010</span></a>). HDPs enhance synthesis of growth factors and cytokines in keratinocytes and epithelial cells that are essential for wound repair (<a href="#Yeung-ATY--Gellatly-SL--Hancock-REW--2011"><span class="Hyperlink">Yeung et al., 2011</span></a>). For example, human LL-37 and HBDs enhances IL-18 secretion from keratinocytes (<a href="#Niyonsaba-F--Ushio-H--Nagaoka-I--Okumura-K--Ogawa-H--2005-"><span class="Hyperlink">Niyonsaba et al., 2005</span></a>). HBD2 and HBD-3 are also actively involved in re-epithelialization of damaged skin (<a href="#Steinmann-J--Halldorsson-S--Agerberth-B--Gudmundsson-GH--2009"><span class="Hyperlink">Steinstraesser et al., 2008</span></a>). Porcine PR-39 is involved in wound healing by increasing the expression of extracellular matrix proteoglycans such as syndecan-1 and 4, which are important for activation of many growth factors (<a href="#Gallo-RL--Ono-M--Povsic-T--Page-C--Eriks"><span class="Hyperlink">Gallo et al., 1994</span></a>). Given such an array of immunomodulatory properties of HDPs, it is highly desirable to harness these properties for antimicrobial therapies to boost host immunity without directly acting on microbes, thereby minimizing the risk of developing resistance (<a href="#Finlay-BB--Hancock-RE--2004-"><span class="Hyperlink">Finlay and Hancock, 2004</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">TRANSCRIPTIONAL REGULATION OF HDPs </p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-2--History-in-MM-" xml:lang="en-GB">HDP Regulation in Humans</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Expression of many HDPs can be induced in response to infection and inflammation. Human cathelicidin LL-37 expression is induced in response to Gram-negative bacteria such as <span class="CharOverride-12">Salmonella enterica</span> serovar Dublin, and enteroinvasive <span class="CharOverride-12">Escherichia coli</span> in human colonic epithelium (<a href="#Hase-K--Eckmann-L--L"><span class="Hyperlink">Hase et al., 2002</span></a>), <span class="CharOverride-12">Helicobacter pylori</span> in human gastric epithelial cells (<a href="#Hase-K--Murakami-2003"><span class="Hyperlink">Hase et al., 2003</span></a>), and <span class="CharOverride-12">Pseudomonas aeruginosa</span> in corneal epithelium (<a href="#Gao-N--Kumar-A--Jyot-J--Yu-FS--20"><span class="Hyperlink">Gao et al., 2010</span></a>). Likewise, the synthesis of LL-37 is increased in response to Gram-positive bacteria including <span class="CharOverride-12">S. aureus</span> in keratinocytes (<a href="#Midorikawa-K--Ouhara-K--Koma"><span class="Hyperlink">Midorikawa et al., 2003</span></a>), <span class="CharOverride-12">Mycobacterium</span> species in human alveolar macrophages, monocytes, neutrophils and epithelial cells (<a href="#Mendez-Samperio-P--Miranda-E--Trejo-A"><span class="Hyperlink">Mendez-Samperio et al., 2008</span></a>; <a href="#Rivas-Santiago-B--Hernandez-Pand"><span class="Hyperlink">Rivas-Santiago et al., 2008</span></a>), LPS and LTA in sinus epithelial cells (<a href="#Nell-MJ--Tjabringa-GS--Vonk-MJ--Hiemstra-PS--Grote-JJ--2004"><span class="Hyperlink">Nell et al., 2004</span></a>), flagellin in corneal epithelial cells (<a href="#Gao-N--Kumar-A--Jyot-J--Yu-FS--20"><span class="Hyperlink">Gao et al., 2010</span></a>). On the other hand, <span class="CharOverride-12">Shigella dysenteriae</span>, <span class="CharOverride-12">Vibrio cholera</span> (<a href="#Islam-D--Bandholtz-L--Nilsson-J--Wigz"><span class="Hyperlink">Islam et al., 2001</span></a>) and <span class="CharOverride-12">Nisseria gonorrhoeae</span> (<a href="#Bergman-P--Johansson-L--Asp-V--Pla"><span class="Hyperlink">Bergman et al., 2005</span></a>) downregulate LL-37 expression in intestinal epithelial cells. In addition, stressors like injury (<a href="#Dorschner-RA--Pestonjamasp-VK"><span class="Hyperlink">Dorschner et al., 2001</span></a>), endoplasmic reticulum stress (<a href="#Park-K--Elias-PM--Oda-Y--Mackenzie-D--Mauro-T--Holleran-WM--Uchida-Y--2011"><span class="Hyperlink">Park et al., 2011</span></a>), and inflammatory disorders (<a href="#Frohm-M--Agerberth-B--Ahangari-G--Stahle-Backdahl-M--Liden-S--Wigzell-H--Gudmundsson"><span class="Hyperlink">Frohm et al., 1997</span></a>) also enhance LL-37 expression in keratinocytes. Moreover, various proinflammatory cytokines (IL-1<span class="CharOverride-10">α</span>, IL-6, and IL-17) (<a href="#Erdag-G--Morgan-JR--2002-"><span class="Hyperlink">Erdag and Morgan, 2002</span></a>; <a href="#Lande-R--Gregorio-J--Facchinett"><span class="Hyperlink">Lande et al., 2007</span></a>; <a href="#Peric-M--Koglin-S--Dombrows"><span class="Hyperlink">Peric et al., 2008</span></a>) and growth factors (insulin-like growth factor 1 and transforming growth factor-<span class="CharOverride-10">α</span> and -<span class="CharOverride-10">β</span>1) (<a href="#Sorensen-OE--Cowland-2003"><span class="Hyperlink">Sorensen et al., 2003</span></a>) promote LL-37 expression in skin epithelial cells, while proinflammatory cytokines display no effect on colonic epithelium (<a href="#Hase-K--Eckmann-L--L"><span class="Hyperlink">Hase et al., 2002</span></a>). IL-10 and IL-13 also suppress LL-37 expression in the skin (<a href="#Kolls-JK--McCray-PB--Jr.--Chan-YR--2008"><span class="Hyperlink">Kolls et al., 2008</span></a>), and IL-18 stimulates LL-37 expression in colonic epithelial cells (<a href="#McDonald-V--Pollok-R"><span class="Hyperlink">McDonald et al., 2006</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Neutrophil-derived human <span class="CharOverride-10">α</span>-defensins are mostly constitutively expressed but inducible in a few cases such as pulmonary tuberculosis, septicemia, and bacterial meningitis (<a href="#Ashitani-J--M-2002"><span class="Hyperlink">Ashitani et al., 2002</span></a>; <a href="#Ashitani-J--Nakaz-2000"><span class="Hyperlink">Ashitani et al., 2000</span></a>; <a href="#Panyutich-A--Shi-J--B-1997"><span class="Hyperlink">Panyutich et al., 1993</span></a>). Similarly, IL-18 and viral infections like hepatitis C increase <span class="CharOverride-10">α</span>-defensin expression in intestinal cells and in peripheral blood mononuclear cells, respectively (<a href="#Aceti-A--Mangoni-ML--Pasquazzi-C--Fi"><span class="Hyperlink">Aceti et al., 2006</span></a>; <a href="#McDonald-V--Pollok-R"><span class="Hyperlink">McDonald et al., 2006</span></a>). HBD1 expression is primarily constitutive, but induced by LPS, and IFN-<span class="CharOverride-10">γ</span> in certain antigen-presenting cells, and repressed by <span class="CharOverride-12">Shigella dyserteriae</span>, <span class="CharOverride-12">Vibrio cholera</span> and bacterial exotoxins (<a href="#Chakraborty-K--Ghosh-S--Koley-H-"><span class="Hyperlink">Chakraborty et al., 2008</span></a>; <a href="#Duits-LA--Ravensbergen-B--Ra"><span class="Hyperlink">Duits et al., 2002</span></a>; <a href="#Islam-D--Bandholtz-L--Nilsson-J--Wigz"><span class="Hyperlink">Islam et al., 2001</span></a>). The expression of HBD2-4 is upregulated by various stimulants including bacteria, and bacterial products, and cytokines such as IL-1<span class="CharOverride-10">α</span>, IL-1<span class="CharOverride-10">β</span>, IL-22, IL-17A, TNF-<span class="CharOverride-10">α</span>, and IFN-<span class="CharOverride-10">γ</span> in keratinocytes (<a href="#Harder-J--Meyer-Hoffert-U--Weh"><span class="Hyperlink">Harder et al., 2004</span></a>). HBD2 and HBD3 are also inducible in <span class="CharOverride-12">Campylobacter jejuni</span>-treated intestinal epithelial cells (<a href="#Zilbauer-M--Dorrell-N--Boughan-PK--Harris-A--Wren-BW--Klein-NJ--Bajaj-Elliott-M--2005"><span class="Hyperlink">Zilbauer et al., 2005</span></a>). Viral infections including HIV-1 and Rhinovirus-16 enhance HBD2 and HBD3 expression in epithelial cells (<a href="#Lehrer-RI--2004"><span class="Hyperlink">Lehrer, 2004</span></a>). <span class="CharOverride-12">Cryptosporidium parvum</span> upregulates HBD2, but down-regulates HBD1 with no effect on HBD3 expression in colonic epithelial cells (<a href="#Zaalouk-TK--Bajaj-Elliott-M--George-JT--M"><span class="Hyperlink">Zaalouk et al., 2004</span></a>).   </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Apart from infection and stress, human LL-37 is also induced by several dietary factors including short-chain fatty acids, flavones, zinc, and vitamin D<span class="CharOverride-14">3</span>. For example, short-chain fatty acids such as butyrate and propionate induce LL-37 expression in human intestinal and hepatic cells as well as lung epithelial cells by acting as histone deacetylase (HDAC) inhibitors (<a href="#Kida-Y--Shimizu-T--Kuwano-K--2006-"><span class="Hyperlink">Kida et al., 2006</span></a>; <a href="#Schauber-J--Iffland-2004"><span class="Hyperlink">Schauber et al., 2004</span></a>; <a href="#Schauber-J--Dorschner-RA--Yama"><span class="Hyperlink">Schauber et al., 2003</span></a>). Other HDAC inhibitors including 4-phenylbutyrate and trichostatin (TSA) are also able to augment LL-37 expression in epithelial and monocytic cells (<a href="#Schauber-J--Iffland-2004"><span class="Hyperlink">Schauber et al., 2004</span></a>; <a href="#Schauber-J--Dorschner-RA--Yama"><span class="Hyperlink">Schauber et al., 2003</span></a>; <a href="#Steinmann-J--Halldorsson-S--Agerberth-B--Gudmundsson-GH--2009"><span class="Hyperlink">Steinmann et al., 2009</span></a>). Other fatty acids including valerate, hexanoate and heptanoate appear to be more potent in inducing LL-37 than butyrate in human colonic and monocytic cells (<a href="#Jiang-WY--Sunkara-LT--Zeng-XF--Deng-Z--Myers-SM--Zhang-GL--2013-."><span class="Hyperlink">Jiang et al., 2013</span></a>). Besides fatty acids, vitamin D<span class="CharOverride-14">3</span> stimulates LL-37 synthesis in lung epithelial cells, keratinocytes, and monocytes, but not in colonic epithelial cells (<a href="#Hansdottir-S--Monick-MM--Hinde-SL--Lovan-N"><span class="Hyperlink">Hansdottir et al., 2008</span></a>; <a href="#Peric-M--Koglin-S--Dombrows"><span class="Hyperlink">Peric et al., 2009</span></a>; <a href="#Schauber-J--Iffland-2004"><span class="Hyperlink">Schauber et al., 200</span></a><span class="Hyperlink">6</span>; <a href="#Schauber-J--Dorschner-RA--Yama"><span class="Hyperlink">Schauber et al., 200</span></a><span class="Hyperlink">8</span>). In addition, zinc has the capacity to enhance LL-37 expression in human intestinal epithelial cells (<a href="#Talukder-P--Satho-T-"><span class="Hyperlink">Talukder et al., 2011</span></a>). LL-37 expression is also augmented by various cyclic adenosine monophosphate (cAMP) signaling agonists in mucosal epithelial cells (<a href="#Chakraborty-K--Ma-2009"><span class="Hyperlink">Chakraborty et al., 2009</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text" xml:lang="en-GB">Human neutrophil <span class="CharOverride-10">α</span>-defensins are induced by 2-arachidonoyl-glycerol and arachidonic acid and the induction is correlated with increased antimicrobial activities of neutrophils against <span class="CharOverride-12">E. coli</span>, <span class="CharOverride-12">S. aureus</span>, herpes simplex virus (HSV)-1, and respiratory syncytial virus (RSV) (<a href="#Chouinard-F--Turcotte-C-"><span class="Hyperlink">Chouinard et al., 2013</span></a>). Human HBD1 expression is mostly constitutive in response to infection, but can be modulated by dietary compounds such as apicidin, butyrate, depudecin, MS-275 and valproic acid in human lung epithelial cell lines through inhibition of HDAC1 (<a href="#Kallsen-K--Andresen-E--Heine-H--2012-"><span class="Hyperlink">Kallsen et al., 2012</span></a>). Another HDAC inhibitor and butyrate analog, 4-phenylbutyrate stimulates the expression of HBD1, but not HBD2-4 in human lung epithelial cells (<a href="#Steinmann-J--Halldorsson-S--Agerberth-B--Gudmundsson-GH--2009"><span class="Hyperlink">Steinmann et al., 2009</span></a>). However, 4-phenylbutyrate fails to induce HBD1 in monocytic cells in the same study (<a href="#Steinmann-J--Halldorsson-S--Agerberth-B--Gudmundsson-GH--2009"><span class="Hyperlink">Steinmann et al., 2009</span></a>), suggesting that HDP regulation is both gene- and cell-specific.  </p>
		  <p class="Body-Text" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">HDAC inhibitors such as TSA, butyrate, and sulforaphane are also capable of enhancing HBD2 expression in human colonic epithelial cells (<a href="#Schwab-M--Reynders-V--Loi"><span class="Hyperlink">Schwab et al., 2008</span></a>). Free fatty acids such as lauric acid, palmitic acid, and oleic acid enhance the antimicrobial activity of sebocytes against <span class="CharOverride-12">Propionibacterium acnes</span> by upregulation of HBD2 (<a href="#Nakatsuji-T--Kao-MC--Zhang-L--Zouboulis-CC--Gallo-RL--Huang-CM--2010-"><span class="Hyperlink">Nakatsuji et al., 2010</span></a>). Zinc and several probiotic bacterial strains have also been found to upregulate HBD2 expression (<a href="#Di-Cagno-R--Mazzac"><span class="Hyperlink">Di Cagno et al., 2010</span></a>; <a href="#Putaala-H--Barrangou-R--Leyer-G"><span class="Hyperlink">Putaala et al., 2010</span></a>; <a href="#Schlee-M--Harder-J--Ko"><span class="Hyperlink">Schlee et al., 2008</span></a>). It is likely that probiotics and prebiotics stimulate bacterial fermentation of short-chain fatty acids, which in turn promote HDP synthesis, host immunity, and disease resistance. </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-2--History-in-MM- ParaOverride-1" xml:lang="en-GB">HDP Regulation in other Species Including Poultry</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Mouse cathelicidin CRAMP expression is enhanced in the skin in response to injury and mild UV irradiation and in mast cells by LPS stimulation (<a href="#Dorschner-RA--Pestonjamasp-VK"><span class="Hyperlink">Dorschner et al., 2001</span></a>; <a href="#Hong-SP--Kim-MJ--Jung-MY--J"><span class="Hyperlink">Hong et al., 2008</span></a>; <a href="#Li-G--Domenico-J--Ji"><span class="Hyperlink">Li et al., 2009a</span></a>). Mouse intestinal <span class="CharOverride-10">α</span>-defensins (cryptidins) are also induced in response to <span class="CharOverride-12">Toxoplasma gondi</span> via TLR9-dependent pathway (<a href="#Foureau-DM--Mielcarz-DW--Menard-LC-"><span class="Hyperlink">Foureau et al., 2010</span></a>). Mouse <span class="CharOverride-10">β</span>-defensin 3 (MBD3) are augmented in the esophagus and tongue by <span class="CharOverride-12">E. coli</span>, and MBD2 expression are triggered in the skin by UV irradiation (<a href="#Ahrens-K--Schunck-M--Podda-GF--Mein"><span class="Hyperlink">Ahrens et al., 2011</span></a>). In contrast, MBD1 expression is inhibited by <span class="CharOverride-12">Cryptosporidium parvum</span> (<a href="#Burd-RS--Furrer-JL--Sullivan-J--Smith-AL--2002-.-Murine-beta-defensin-3-is-an-in"><span class="Hyperlink">Burd et al., 2002</span></a>; <a href="#Hong-SP--Kim-MJ--Jung-MY--J"><span class="Hyperlink">Hong et al., 2008</span></a>; <a href="#Zaalouk-TK--Bajaj-Elliott-M--George-JT--M"><span class="Hyperlink">Zaalouk et al., 2004</span></a>). In rats, neuropathogenic <span class="CharOverride-12">E. coli</span> enhances the expression of intestinal <span class="CharOverride-10">α</span>-defensins (<a href="#Birchenough-GM--Johansson"><span class="Hyperlink">Birchenough et al., 2013</span></a>), and methicillin-resistant <span class="CharOverride-12">Staphylococcus aureus</span> enhanced the rat <span class="CharOverride-10">β</span>-Defensin 3 (RBD3) expression in the lung (<a href="#Wu-Q--Gui-P--Ya-2011"><span class="Hyperlink">Wu et al., 2011</span></a>). In response to intestinal ischemia or injury, RBD2 is stimulated in the lung as well (<a href="#Liu-KX--Chen-SQ--Zh"><span class="Hyperlink">Liu et al., 2009</span></a>). Similarly, <span class="CharOverride-12">Actinobacillus actinomycetemcomitans</span> increases RBD1 and RBD2 expression in gingival epithelia (<a href="#Kurland-AR--Schreiner-H--Diamond-G--2006"><span class="Hyperlink">Kurland et al., 2006</span></a>). Testicular and epididymal <span class="CharOverride-10">β</span>-defensins are enhanced in rats treated with LPS (<a href="#Biswas-B--Yenugu-S--2013"><span class="Hyperlink">Biswas and Yenugu, 2013</span></a>, <a href="#Biswas-B--Yenugu-S--2011"><span class="Hyperlink">2011</span></a>). In rabbits, oral supplementation of butyrate or 4-phenylbutyrate alleviates clinical symptoms of dysentery in shigellosis infections through upregulation of cathelicidin expression in the colon and lung epithelia (<a href="#Raqib-R--Sarker-P--Bergman"><span class="Hyperlink">Raqib et al., 2006</span></a>; <a href="#Sarker-P--Ahmed-S--Tiash-S-"><span class="Hyperlink">Sarker et al., 2011</span></a>).</p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Like their mammalian counter parts, porcine cathelicidins such as protegrins and PR-39 show an increased expression in porcine bone marrow cells in response to different <span class="CharOverride-12">Salmonella</span> strains, LPS, and IL-6 (<a href="#Wu-Q--Gui-P--Ya-2011"><span class="Hyperlink">Wu et al., 2011</span></a>; <a href="#Zhang-G--Ross-1997"><span class="Hyperlink">Zhang et al., 1997</span></a>). In addition, PR-39 is increased in mucosal and lymphatic tissues of the respiratory tract in pigs chronically, but not acutely infected with <span class="CharOverride-12">Actinobacillus pleuropneumoniae</span> (<a href="#Hennig-Pauka-I--Koch-R--Hoelt"><span class="Hyperlink">Hennig-Pauka et al.</span></a><span class="Hyperlink">,  2012</span>). Porcine <span class="CharOverride-10">β</span>-defensin 2 (PBD2) expression is enhanced in intestinal epithelial cells exposed to live <span class="CharOverride-12">Salmonella</span>, but not heat-killed or colistin-treated bacteria (<a href="#Veldhuizen-EJ--Hend-2006"><span class="Hyperlink">Veldhuizen et al., 2006</span></a>). Likewise, <span class="CharOverride-12">Salmonella enteritidis</span> infection stimulates PBD1 gene expression (<a href="#Veldhuizen-EJ--Hend-2006"><span class="Hyperlink">Veldhuizen et al., 2006</span></a>; <a href="#Veldhuizen-EJ--Koo-2009"><span class="Hyperlink">Veldhuizen et al., 2009</span></a>), while PBD1 is upregulated and PBD2 is down-regulated in intestinal epithelial cells treated with <span class="CharOverride-12">Fusarium</span> toxin (<a href="#Wan-ML--Woo-CS--Allen-KJ--Turner-PC--El-Nezami-H--2013-"><span class="Hyperlink">Wan et al., 2013</span></a>). Treatment of primary tracheal epithelial cells with LPS or canine respiratory coronavirus or parainfluenza virus has led to a decreased expression of several canine <span class="CharOverride-10">β</span>-defensins (<a href="#Erles-K--Brownlie-J--2010-"><span class="Hyperlink">Erles and Brownlie, 2010</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text" xml:lang="en-GB">In ruminant animals, <span class="CharOverride-12">E. coli</span> or LPS stimulation of neutrophils results in an increased production of bovine cathelicidin Bac-5 (<a href="#Tomasinsig-L--Scocchi-M--Di-L"><span class="Hyperlink">Tomasinsig et al., 2002</span></a>). Furthermore, bovine HDPs such as TAP, LAP, and BBD5 are upregulated in response to infections, particularly in the mammary, lung, and uterine tissues (<a href="#Meade-KG--Cormican-P-"><span class="Hyperlink">Meade et al., 2014</span></a>). Several bovine <span class="CharOverride-10">β</span>-defensins are also increased in response to inflammation and infection (<a href="#Das-H--Swamy-N--Sa"><span class="Hyperlink">Das et al., 2008</span></a>; <a href="#Russell-JP--Diamond-G--Tarver-AP--Scanlin-TF--Bevins-CL--1996"><span class="Hyperlink">Russell et al., 1996</span></a>; <a href="#Stolzenberg-ED--Anderson-GM--Ack"><span class="Hyperlink">Stolzenberg et al., 1997</span></a>). Similarly, <span class="CharOverride-12">S. aureus</span> or LPS treatment of umbilical endothelial cells potentiates the expression of bovine LAP, BBD1 and BBD4 through autocrine production of TNF-<span class="CharOverride-10">α</span> (<a href="#Alva-Murillo-N--T-2012b"><span class="Hyperlink">Alva-Murillo et al., 2012b</span></a>). Intrauterine infusion of <span class="CharOverride-12">E. coli</span> in goats results in up-regulation of <span class="CharOverride-10">β</span>-defensin 2 gene expression (<a href="#Shao-CY--Wang-H--Meng-X--Zhu-JQ-"><span class="Hyperlink">Shao et al., 2012</span></a>), whereas infection of intestinal epithelial cells with <span class="CharOverride-12">Eimeria spp</span> leads to down-regulation of the goat <span class="CharOverride-10">β</span>-defensin 2 gene (<a href="#Ibarra-Velarde-F--Alcala-Canto-Y--2007"><span class="Hyperlink">Ibarra-Velarde and Alcala-Canto, 2007</span></a>). In sheep, SBD1 is increased with parainfluenza virus type 3 infection and decreased by <span class="CharOverride-12">Mannheimia haemolytica</span>, with no difference in gene expression observed with SBD2 (<a href="#Ackermann-MR--Gallup-JM--Zabner-J--Evan"><span class="Hyperlink">Ackermann et al., 2004</span></a>). </p>
		  <p class="Body-Text" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">In avian species, HDPs are also differentially expressed in response to infectious agents and inflammatory mediators (<a href="#Cuperus-T--Coorens-M--van"><span class="Hyperlink">Cuperus et al., 2013</span></a>; <a href="#Zhang-G--Sunkara-LT--2014"><span class="Hyperlink">Zhang and Sunkara, 2014</span></a>). For example, several chicken cathelicidins are augmented in response to <span class="CharOverride-12">S. typhimurium</span> in cecal tonsils, and down-regulated by <span class="CharOverride-12">Camphylobacter jejuni</span> in peripheral blood leukocytes and <span class="CharOverride-12">Eimeria praecox</span> in small intestine (<a href="#Akbari-MR--Haghighi-HR--Chambers"><span class="Hyperlink">Akbari et al., 2008</span></a>; <a href="#Meade-KG--Cormican-P-"><span class="Hyperlink">Meade et al., 2009</span></a>; <a href="#Sumners-LH--Miska-KB--Jen"><span class="Hyperlink">Sumners et al., 2011</span></a>). Chicken <span class="CharOverride-10">β</span>-defensins are also regulated by <span class="CharOverride-12">Haemophilus paragallinarum</span> in the trachea (AvBD3) and by <span class="CharOverride-12">Salmonella typhimurium </span>(AvBD1, 2, 5, and 6) in cecal tonsils (<a href="#Akbari-MR--Haghighi-HR--Chambers"><span class="Hyperlink">Akbari et al., 2008</span></a>; <a href="#Zhao-C--Nguyen-T--Liu-L--Sacco-RE--Brogden-KA--Lehrer-RI--2001"><span class="Hyperlink">Zhao et al., 2001</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Dietary compounds has also been found to regulate HDPs expression in non-human species. For example, fatty acids such as butyrate, propionate and hexanoate have been shown to increase the expression of several bovine <span class="CharOverride-10">β</span>-defensins in primary mammary epithelial cells and inhibit both internalization and infection of <span class="CharOverride-12">Staphylococcus aureus</span> (<a href="#Alva-Murillo-N--O-2012a"><span class="Hyperlink">Alva-Murillo et al., 2012a</span></a>). In contrast, the expression of bovine LAP, TAP, and BBD4 is decreased in rumen epithelia when infused with butyrate (<a href="#Baldwin-RLt--Wu-S--Li-W--Li"><span class="Hyperlink">Baldwin et al., 2012</span></a>). Oleic acid induces MBD4 in the hair follicle sebaceous glands of ear skin in mice (<a href="#Nakatsuji-T--Kao-MC--Zhang-L--Zouboulis-CC--Gallo-RL--Huang-CM--2010-"><span class="Hyperlink">Nakatsuji et al., 2010</span></a>). Lysozyme-digested probiotics increases mouse CRAMP expression in macrophages and protects rats against sepsis (<a href="#Bu-HF--Wang-X--Zhu-YQ-"><span class="Hyperlink">Bu et al., 2006</span></a>). Free fatty acids with 3-8 carbons are able to induce porcine HDPs such as PBD2, PBD3, PEP2C, and protegrins in intestinal epithelial cells, alveolar macrophages, and primary monocytes (<a href="#Zeng-X--Sunkara-LT--Jiang-W--Bible-M--Carter-S--Ma-X--Qiao-S--Zhang-G--2013"><span class="Hyperlink">Zeng et al., 2013</span></a>). PBD2 is induced in the ileum of pigs administered with a probiotic, <span class="CharOverride-12">Lactobacillus rhamnosus</span> (<a href="#Li-XQ--Zhu-Y-2012"><span class="Hyperlink">Li et al., 2012</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">In animal agriculture, particularly in poultry, organic acids including butyrate and propionate have been used for decades and shown an overall improved resistance to <span class="CharOverride-12">S. enteritidis</span> (<a href="#Van-Immerseel-F--Ru-2006"><span class="Hyperlink">Van Immerseel et al., 2006</span></a>) and <span class="CharOverride-12">Clostridium perfringens</span> (<a href="#Timbermont-L--Lanckriet-A--De"><span class="Hyperlink">Timbermont et al., 2010</span></a>). Many antibacterial mechanisms of organic acids have been proposed, including a reduction of intestinal pH, direct antibacterial activities, and suppression of bacterial attachment to host intestinal cells (<a href="#Gantois-I--Ducatelle-R--Pasmans-F--Haesebrou"><span class="Hyperlink">Gantois et al., 2006</span></a>; <a href="#Van-Immerseel-F--De-2004"><span class="Hyperlink">Van Immerseel et al., 2004</span></a>; <a href="#Van-Immerseel-F--De-2003"><span class="Hyperlink">Van Immerseel et al., 2003</span></a>; <a href="#Van-Immerseel-F--Ru-2006"><span class="Hyperlink">Van Immerseel et al., 2006</span></a>). Augmenting HDP synthesis and host immunity has also been proposed as a new mode of action of organic acids, which often contain short-chain fatty acids that have been revealed to be strong inducers of chicken HDPs both <span class="CharOverride-12">in vitro</span> and <span class="CharOverride-12">in vivo</span> (<a href="#Sunkara-LT--Achanta-2011"><span class="Hyperlink">Sunkara et al., 2011</span></a>; <a href="#Sunkara-LT--Jiang-2012"><span class="Hyperlink">Sunkara et al., 2012</span></a>). A combination of three short-chain fatty acids, namely butyrate, acetate and propionate, could synergistically induce chicken HDP expression and clearance of <span class="CharOverride-12">Salmonella</span> in the cecum of chickens (<a href="#Sunkara-LT--Jiang-2012"><span class="Hyperlink">Sunkara et al., 2012</span></a>). A phytochemical, forskolin, also synergizes with butyrate in enhancing chicken HDP expression both <span class="CharOverride-12">in vitro</span> and <span class="CharOverride-12">in vivo</span> (<a href="#Sunkara-LT--Jiang-2012"><span class="Hyperlink">Sunkara et al., 2012</span></a>; <a href="#Sunkara-LT--Zeng-2014"><span class="Hyperlink">Sunkara et al., 2014</span></a>). </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">CONCLUSIONS</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">HDPs are important effector molecules of innate immunity, possessing a myriad of beneficial functions with potent antimicrobial, antiinflammatory, and immunomodulatory activities. HDPs are mobilized quickly in response to infection and inflammation. A growing body of evidence suggests that dietary factors including vitamin D<span class="CharOverride-14">3</span>, short-chain fatty acids, zinc, certain amino acids, and phytochemicals are capable of inducing HDP synthesis in humans and other animal species like cattle, pigs, sheep and poultry, suggesting the potential of using these HDP-inducing compounds for immune augmentation and disease resistance. Dietary modulation of the endogenous HDP synthesis may be further explored as a novel antibiotic-free strategy for disease prevention and control for both human and animal health including poultry. </p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">ACKNOWLEDGMENTS</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">We thank all the members of the Zhang Laboratory for their valuable contributions to successfully complete different research projects in studying HDP modulation. The research on host defence peptides in different animals in the Zhang Laboratory is supported by the U.S. Department of Agriculture grant (2008-35204-04544), Oklahoma Center for the Advancement of Science and Technology grants HR07-113, HR12-051,  AR07.2-087 and AR12.2-077), and Oklahoma Agricultural Experiment Station project (H-2811). The funders has no role in preparation of this review article.</p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">CONFLICTS OF INTEREST</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">The authors have declared no conflict of interest.</p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
			<p class="Heading-1--Introduction----" xml:lang="en-GB">Author’s Contribution</p>
		  <p class="Heading-1--Introduction----" xml:lang="en-GB">&nbsp;</p>
			<p class="Body-Text ParaOverride-1" xml:lang="en-GB">Lakshmi Tulasi Sunkara and Amanda Renee Curits drafted the manuscript and Guolong Zhang drafted and revised the manuscript.</p>
		  <p class="Body-Text ParaOverride-1" xml:lang="en-GB">&nbsp;</p>
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