Porcine |
Cathelicidin—Proline-Arginine-39 (PR-39) |
Block the recruitment of neutrophils through the inhibition of ubiquitin proteasome-mediated IkBα degradation on endothelial cells |
Intestinal cells, bone marrow, lymphoid tissues, and leukocytes |
|
β-Defensins |
Creating pores on the microbial membrane surface to increase cellular permeability |
Tissues and cells of the immune system |
|
Creopins |
Modulate membrane permeability by forming partially selective ion channels, or binding to negatively charged membrane lipids to form a closely packed layer that renders membranes permeable |
Small intestine |
Bovine |
Cathelicidins (synthetic endogenous-source)—Bovine myeloid antimicrobial peptides (BMAPs), Bac2A, and IDR-1018 |
Antibacterial activity against pathogens |
Different tissues of the body and milk |
|
β-Defensin—Tracheal antimicrobial peptide (TAP) |
Prevent infection at the respiratory mucosal surfaces through bactericidal activities |
Epithelial cells lining the respiratory tract and other mucosal surfaces |
Poultry |
Cathelicidins, namely chCATH-1, −2 −3 (also called fowlicidin-1, −2 and −3), |
Exert antibacterial activity by serving as a chemo-attractant to neutrophils, without affecting the migration of monocytes or lymphocytes |
Lymphoid tissues in chickens |
|
β-Defensins—AvBD1 toAvBD14 |
Provides broad-spectrum antimicrobial activity |
Expressed in various tissues, including the reproductive organs, bone marrow, respiratory tract, skin, digestive tract, and in cells like heterophils |
|
Ovodefensins |
Antibacterial activity against E. coli and S. aureus
|
Expressed throughout the chicken oviduct |
|
Gallin |
Antibacterial activity against E. coli
|
Found in egg albumen |
Fish |
Piscidins |
Bacteriostatic—inhibit further growth and development of pathogens by penetrating and destroying the spores |
Various tissues in the fish |
|
β-Defensins |
Contributes to antimicrobial activity in phagocytes |
Various tissues in the fish |
|
Cathelicidin |
Antibacterial |
Embryonic tissue in fish |
|
Hepcidins—Hemp1 and Hemp2 |
Increase resistance to microbial infection by preventing the release of iron from macrophages, and preventing the absorption of iron in the small intestine |
Predominantly expressed in the liver of adult fish |
|
Histone-derived peptides |
Broad-spectrum antibacterial activity |
In Fish |