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 Microhyla heymonsivogt 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. © 2021, Chai et al.

Citation

Jinwei Chai, Xin Chen, Tiaofei Ye, Baishuang Zeng, Qingye Zeng, Jiena Wu, Barbora Kascakova, Larissa Almeida Martins, Tatyana Prudnikova, Ivana Kuta Smatanova, Michail Kotsyfakis, Xueqing Xu. Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties. eLife. 2021 Apr 20;10

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PMID: 33875135

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