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

0554069 - BC 2022 RIV GB eng J - Článek v odborném periodiku
Chai, J. - Chen, X. - Ye, T. - Zeng, B. - Zeng, Q. - Wu, J. - Kaščáková, B. - Martins, Larissa Almeida - Prudníková, T. - Smatanová, I. - Kotsyfakis, Michalis - Xu, X.
Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.
eLife. Roč. 10, APR 20 2021 (2021), č. článku e64411. ISSN 2050-084X. E-ISSN 2050-084X
Institucionální podpora: RVO:60077344
Klíčová slova: antimicrobial peptides * cathelicidin * immunology
Obor OECD: Microbiology
Impakt faktor: 8.713, rok: 2021
Způsob publikování: Open access
https://elifesciences.org/articles/64411

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 alpha-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, beta-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.
Trvalý link: http://hdl.handle.net/11104/0328688