Antimicrobial Peptides in Farm Animals: An Updated Review on Its Diversity, Function, Modes of Action and Therapeutic Prospects
Abstract
:1. Introduction
2. Structural Diversity Among AMPs
3. Biological Function and Mode of Action
4. Bovine AMPs
4.1. Bovine Cathelicidins
4.1.1. Indolicidin
4.1.2. Bovine MyeloidAntimicrobialPeptides (BMAPs)
BMAP-27
BMAP-28
BMAP-18
BMAP-34
4.2. Bovine β-Defensins
4.2.1. Tracheal Antimicrobial Peptide (TAP)
4.2.2. Lingual Antimicrobial Peptide (LAP)
4.2.3. BNBD (Bovine Neutrophil β-Defensins)
4.2.4. Enteric β–Defensins
4.2.5. Bovine β-Defensin 1
4.3. Bovine Psoriasin
4.4. Proline-Rich AMPs: Bac-5 and Bac-7
5. Equine AMPs
5.1. Equine Cathelicidin
5.2. Equine Neutrophil Antimicrobial Peptides
5.3. Equine Hepcidin
5.4. Equine α and β Defensin
6. Porcine AMPs
6.1. Porcine Cathelicidins
6.1.1. Protegrins
6.1.2. PR39
6.1.3. Prophenin 1
6.1.4. Cecropin P1
6.1.5. Porcine Myeloid Antimicrobial Peptide
6.2. Porcine β Defensin
7. CaprineAMPs
8. Ovine AMPs
8.1. Ovine Cathelicidins
8.2. Ovine β-Defensins
9. Milk-Derived AMPs
AMPs | Source | Activity | Structure | Mode of Action |
---|---|---|---|---|
CATHELICIDIN | ||||
Indolicidin | Bovine neutrophils [58] | Gram-positive and Gram-negative bacteria, yeast, and fungi [59,62,63] | Extended helix [24,25] | Membrane thinning, disruption of the membrane by channel formation, inhibition of DNA synthesis, and topoisomerase 1 [24,41,42,43,44,45] |
BMAP-18, BMAP-27, BMAP-28,and BMAP-34 | Bovine myeloid cells [40] | Gram-positive and Gram-negative bacteria, viruses, fungi, trypanosomes, and tumor cells [40,64,65,66,67,68,71,72,75,76] | α-helix [9,76] | Formation of small channels in the bacterial membrane resulting in the release of small ions, transition pores in mitochondria, and LPS neutralization [9,40,69,73,74], |
Bac-5 and Bac-7 | Bovine neutrophil [101] | Gram-positive and Gram-negative bacteria [101] | Combination of α-helix and β-sheet [27] | Inhibits protein synthesis by entering via bacterial inner membrane transporter SbmA and YjiL/MdtM [102,103] |
eCATH1, eCATH2, and eCATH3 | Equine neutrophils [14] | Broad-spectrum [14,106,107] | α-helix [14] | N.A. |
Protegrin | Porcine Lung and intestine [121] | Gram-positive and Gram-negative bacteria, PRRSV, and yeast [18,119,121,122,124,125,126,127,128,135] | β-sheet [17,18,19,20] | Pore formation in the bacterial cell membrane and immunomodulation [120,129] |
PR-39 | Porcine intestine, upper and lower respiratory tract [137] | Gram-negative bacteria and Mycobacterium tuberculosis [144,145,146] | Combination of α-helix and β-sheet [27] | Halts DNA and protein synthesis by exerting proteolytic activity and acts as a calcium-dependent chemoattractant for neutrophil [40,143,144] |
Prophenin 1 | Porcine leukocytes [147] | More effective against Gram-negative bacteria and less effective against Gram-positive bacteria [147,148] | β-sheet (homology modeling) | N.A. |
Cecropin P1 | Porcine small intestine [150] | Gram-positive, Gram-negative bacteria and viruses [152,153,154] | α-helix [12,13] | Disruption of lipid bilayer using the carpet model [12,34] |
PMAPs | Porcine bone marrow [155] | Gram-positive and Gram-negative bacteria, fungi, and nematodes [155,156,157,158] | α-helix [11] | Permeabilize bacterial membrane [155,156,157] |
ChBac3 and ChBac5 | Caprine leucocytes [164] | Broad-spectrum [164,166] | N.A. | Membrane disruption [165] |
OaBac5, OaBac7, and variants | Ovine leucocytes [164] | Broad-spectrum [164,168] | N.A. | depolarization of the cytoplasmic membranes [168] |
SMAP29 | Ovine myeloid cells [10] | Gram-positive and Gram-negative bacteria and yeast [169] | α-helix [10] | Permeabilize bacterial membrane [35] |
DEFENSINS | ||||
TAP | Bovine mucosal epithelial cells and mammary epithelial cells [77,78] | Broad-spectrum [77,81,82,83] | β-sheet (homology modeling) | N.A. |
LAP | Bovine squamous epithelial cells tongue, esophagus, rumen reticulum, omasum, and chief cells of gastric glands [85,86,87] | Broad-spectrum [84] | β-sheet (homology modeling) | N.A. |
BNBDs | Bovine neutrophils alveolar tissue and pulmonary macrophages [96,97] | Broad-spectrum [94,96] | β-sheet (homology modeling) | N.A. |
EBD | Bovine epithelial cells of intestine and colon [99] | Cryptosporidium parvum [99] | N.A. | N.A. |
Bovine β-defensin 1 | Urogenital tract [100] | Strong response against Gram-negative bacteria as compared to Gram-positive bacteria [100] | β-sheet (homology modeling) | |
Equine β defensin 1 | Hepatic tissue and respiratory epithelial tissue [114,115] | Broad-spectrum [115] | N.A | N.A |
Equine α-defensin DEFA1 | Small intestine [116] | Gram-positive andgram-negative bacteriaandfungi [116,117] | β-sheet | membrane permeabilization |
Porcine β Defensin | Tongue, liver, kidney, small intestine, and large intestine [163] | Broad-spectrum [160,161,162] | β-sheet (homology modeling) | N.A. |
Ovine β-defensin (SBD1 and SBD2) | Trachea, tongue, and gastrointestinal tract [167] | Gram-positive and Gram-negative bacteria, parainfluenza virus, and M. haemolytica [167,171,172] | β-sheet (homology modeling) | N.A. |
NEUTROPHIL ANTIMICROBIAL PEPTIDE | ||||
eNAP-1 and eNAP-2 | Equine neutrophils [108] | Broad-spectrum [108,109,110] | N.A. | Selective activity against microbial serine proteases [109,110] |
PSORIASIN | ||||
Bovine Psoriasin | Udder | Gram-negative bacteria [47] | N.A. | Reduces bacterial survival by zinc sequestration [47] |
HEPCIDIN | ||||
Equine hepcidin | Liver [111] | N.A. | N.A. | Induces hypoferrimia by iron sequestration [46,112] |
10. Therapeutic Potential of Farm Animal-Derived AMPs
11. Conclusions
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
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AMPs | Source | Clinical Phase | Indication | Administration | Clinical Identifier |
---|---|---|---|---|---|
MBI-226Omignan | Indolicidin(Bovine) | Phase III | Prevention of local catheter site infection and colonization in patients with central venous catheters | Topical gel | NCT00231153 |
CLS001Omignan | Phase III | Severe papulopustular rosacea | Topical gel | NCT02576860 | |
MX942 (SGX942) | Phase III | Immunomodulation during oral mucositis | Intravenous infusion | NCT03237325 | |
Omignan | Phase II | Seborrheic Dermatitis | Topical Gel | NCT03688971 | |
IB-367Isegnan | Protegrin-1 Derivative | Phase III | Oral mucositis in the patient receiving radiation therapy for head and neck cancer | Oral solution | NCT00022373 |
POL7080 | Protegrin-1Analog | Phase II | Non-cystic fibrosis bronchiectasis caused by Pseudomonas aeruginosa infection. | Intravenous infusion | NCT02096328 |
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Kumar, R.; Ali, S.A.; Singh, S.K.; Bhushan, V.; Mathur, M.; Jamwal, S.; Mohanty, A.K.; Kaushik, J.K.; Kumar, S. Antimicrobial Peptides in Farm Animals: An Updated Review on Its Diversity, Function, Modes of Action and Therapeutic Prospects. Vet. Sci. 2020, 7, 206. https://doi.org/10.3390/vetsci7040206
Kumar R, Ali SA, Singh SK, Bhushan V, Mathur M, Jamwal S, Mohanty AK, Kaushik JK, Kumar S. Antimicrobial Peptides in Farm Animals: An Updated Review on Its Diversity, Function, Modes of Action and Therapeutic Prospects. Veterinary Sciences. 2020; 7(4):206. https://doi.org/10.3390/vetsci7040206
Chicago/Turabian StyleKumar, Rohit, Syed Azmal Ali, Sumit Kumar Singh, Vanya Bhushan, Manya Mathur, Shradha Jamwal, Ashok Kumar Mohanty, Jai Kumar Kaushik, and Sudarshan Kumar. 2020. "Antimicrobial Peptides in Farm Animals: An Updated Review on Its Diversity, Function, Modes of Action and Therapeutic Prospects" Veterinary Sciences 7, no. 4: 206. https://doi.org/10.3390/vetsci7040206