Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties

Antimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of frog. Cath-MH has a single α-helical structure in membr...

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Veröffentlicht in:eLife 2021-04, Vol.10
Hauptverfasser: Chai, Jinwei, Chen, Xin, Ye, Tiaofei, Zeng, Baishuang, Zeng, Qingye, Wu, Jiena, Kascakova, Barbora, Martins, Larissa Almeida, Prudnikova, Tatyana, Smatanova, Ivana Kuta, Kotsyfakis, Michail, Xu, Xueqing
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Sprache:eng
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Zusammenfassung:Antimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of frog. Cath-MH has a single α-helical structure in membrane-mimetic environments and is antimicrobial against fungi and bacteria, especially Gram-negative bacteria. In contrast to other cathelicidins, cath-MH suppresses coagulation by affecting the enzymatic activities of tissue plasminogen activator, plasmin, β-tryptase, elastase, thrombin, and chymase. Cath-MH protects against lipopolysaccharide (LPS)- and cecal ligation and puncture-induced sepsis, effectively ameliorating multiorgan pathology and inflammatory cytokine through its antimicrobial, LPS-neutralizing, coagulation suppressing effects as well as suppression of MAPK signaling. Taken together, these data suggest that cath-MH is an attractive candidate therapeutic agent for the treatment of septic shock.
ISSN:2050-084X
2050-084X
DOI:10.7554/eLife.64411