Jinwei Chai: Department of Respiratory Medicine, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Xin Chen: Department of Respiratory Medicine, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Tiaofei Ye: Department of Respiratory Medicine, Zhujiang Hospital, Southern Medical University, Guangzhou, China.
Baishuang Zeng: Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
Qingye Zeng: Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
Jiena Wu: Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China.
Barbora Kascakova: Faculty of Science, University of South Bohemia in Ceske Budejovice, Branisovska, Czech Republic.
Larissa Almeida Martins: Institute of Parasitology, Biology Center of the Czech Academy of Sciences, Branisovska, Czech Republic. ORCID
Tatyana Prudnikova: Faculty of Science, University of South Bohemia in Ceske Budejovice, Branisovska, Czech Republic.
Ivana Kuta Smatanova: Faculty of Science, University of South Bohemia in Ceske Budejovice, Branisovska, Czech Republic. ORCID
Michail Kotsyfakis: Institute of Parasitology, Biology Center of the Czech Academy of Sciences, Branisovska, Czech Republic. ORCID
Xueqing Xu: Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China. ORCID
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.
