2mxq
From Proteopedia
The solution structure of DEFA1, a highly potent antimicrobial peptide from the horse
Structural highlights
FunctionDEFA1_HORSE Has broad-spectrum antimicrobial properties (PubMed:17620056, PubMed:19211153). The antimicrobial activity decreases in the present of salt in vitro (PubMed:19211153). Binds anionic phospholipids, which leads to the aggregation of liposomes in vitro (PubMed:25769951). Membrane permeabilization of the target cells is an essential part of the peptide's mode of antimicrobial activity (PubMed:17620056, PubMed:22232283). No hemolytic activity against sheep or horse erythrocytes (PubMed:22232283). Has antibacterial activity against the bacterial horse pathogens Gram-positive R.equi ATCC 33701 P(-) (minimum bactericidal concentration or MBC=5 ug/ml) and R.equi ATCC 33701 P(+) (MBC=5 ug/ml), which are resistant against beta-lactam antibiotics. Also has antibacterial activity against highly infectious wild-type strain R.equi 85F P(+) (MBC=5 ug/ml), S.equi subsp. equi (MBC=5 ug/ml), S.equi subsp. zooepidemicus (MBC=5 ug/ml), S.dysgalactiae subsp. equisimilis (MBC=10 ug/ml), S.choleraesuis subsp. choleraesuis serovar Typhimurium (MBC=10 ug/ml), and P.multocida subsp. multocida (MBC=>10 ug/ml) (PubMed:19211153). Probably contributes to the antimicrobial barrier function of the small bowel mucosa (Probable).[1] [2] [3] [4] Publication Abstract from PubMedDefensins are small effector molecules of the innate immune system that are present in almost all organisms including plants and animals. These peptides possess antimicrobial activity against a broad range of microbes including bacteria, fungi and viruses and act as endogenous antibiotics. alpha-Defensins are a subfamily of the defensin family and their expression is limited to specific tissues. Equine DEFA1 is an enteric alpha-defensin exclusively secreted by Paneth cells and shows an activity against a broad spectrum of microbes, including typical pathogens of the horse such as Rhodococcus equi, various streptococci strains, Salmonella choleraesuis, and Pasteurella multocida. Here, we report the three-dimensional structure of DEFA1 solved by NMR-spectroscopy and demonstrate its specific function of aggregating various phospholipids. Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1.,Michalek M, Jung S, Shomali MR, Cauchard S, Sonnichsen FD, Grotzinger J Biochem Biophys Res Commun. 2015 Apr 17;459(4):668-72. doi:, 10.1016/j.bbrc.2015.02.168. Epub 2015 Mar 11. PMID:25769951[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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