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

作者：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^*

来源：eLife, 2021, 10: e64411.

DOI：10.7554/eLife.64411

• MOLECULAR-REPLACEMENT
• ATTENUATES SEPSIS
• LL-37
• IDENTIFICATION
• MECHANISMS
• MEDIATORS
• MODELS
• GENE

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.

• 单位
  南方医科大学