Cargando…

King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates

Cationic antimicrobial peptides (AMPs) are considered as important candidate therapeutic agents, which exert potent microbicidal properties against bacteria, fungi and some viruses. Based on our previous findings king cobra cathelicidin (OH-CATH) is a 34-amino acid peptide that exerts strong antibac...

Descripción completa

Detalles Bibliográficos
Autores principales: Zhao, Feng, Lan, Xin-Qiang, Du, Yan, Chen, Pei-Yi, Zhao, Jiao, Zhao, Fang, Lee, Wen-Hui, Zhang, Yun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Science Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5885386/
https://www.ncbi.nlm.nih.gov/pubmed/29515090
http://dx.doi.org/10.24272/j.issn.2095-8137.2018.025
_version_ 1783311976285339648
author Zhao, Feng
Lan, Xin-Qiang
Du, Yan
Chen, Pei-Yi
Zhao, Jiao
Zhao, Fang
Lee, Wen-Hui
Zhang, Yun
author_facet Zhao, Feng
Lan, Xin-Qiang
Du, Yan
Chen, Pei-Yi
Zhao, Jiao
Zhao, Fang
Lee, Wen-Hui
Zhang, Yun
author_sort Zhao, Feng
collection PubMed
description Cationic antimicrobial peptides (AMPs) are considered as important candidate therapeutic agents, which exert potent microbicidal properties against bacteria, fungi and some viruses. Based on our previous findings king cobra cathelicidin (OH-CATH) is a 34-amino acid peptide that exerts strong antibacterial and weak hemolytic activity. The aim of this research is to evaluate the efficacy of both OH-CATH30 and its analog D-OH-CATH30 against clinical isolates comparing with routinely utilized antibiotics in vitro. In this study, 584 clinical isolates were tested (spanning 2013–2016) and the efficacy of the candidate peptides and antibiotics were determined by a broth microdilution method according to the CLSI guidelines. Among the 584 clinical isolates, 85% were susceptible to OH-CATH30 and its analogs. Both L- and D-OH-CATH30 showed higher efficacy against (toward) Gram-positive bacteria and stronger antibacterial activity against nearly all Gram-negative bacteria tested compare with antibiotics. The highest bactericidal activity was detected against Acinetobacter spp., including multi-drug-resistant Acinetobacter baumannii (MRAB) and methicillin-resistant Staphylococcus aureus (MRSA). The overall efficacy of OH-CATH30 and its analogs was higher than that of the 9 routinely used antibiotics. OH-CATH30 is a promising candidate drug for the treatment of a wide variety of bacterial infections which are resistant to many routinely used antimicrobial agents.
format Online
Article
Text
id pubmed-5885386
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher Science Press
record_format MEDLINE/PubMed
spelling pubmed-58853862018-04-12 King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates Zhao, Feng Lan, Xin-Qiang Du, Yan Chen, Pei-Yi Zhao, Jiao Zhao, Fang Lee, Wen-Hui Zhang, Yun Zool Res Article Cationic antimicrobial peptides (AMPs) are considered as important candidate therapeutic agents, which exert potent microbicidal properties against bacteria, fungi and some viruses. Based on our previous findings king cobra cathelicidin (OH-CATH) is a 34-amino acid peptide that exerts strong antibacterial and weak hemolytic activity. The aim of this research is to evaluate the efficacy of both OH-CATH30 and its analog D-OH-CATH30 against clinical isolates comparing with routinely utilized antibiotics in vitro. In this study, 584 clinical isolates were tested (spanning 2013–2016) and the efficacy of the candidate peptides and antibiotics were determined by a broth microdilution method according to the CLSI guidelines. Among the 584 clinical isolates, 85% were susceptible to OH-CATH30 and its analogs. Both L- and D-OH-CATH30 showed higher efficacy against (toward) Gram-positive bacteria and stronger antibacterial activity against nearly all Gram-negative bacteria tested compare with antibiotics. The highest bactericidal activity was detected against Acinetobacter spp., including multi-drug-resistant Acinetobacter baumannii (MRAB) and methicillin-resistant Staphylococcus aureus (MRSA). The overall efficacy of OH-CATH30 and its analogs was higher than that of the 9 routinely used antibiotics. OH-CATH30 is a promising candidate drug for the treatment of a wide variety of bacterial infections which are resistant to many routinely used antimicrobial agents. Science Press 2018-03-07 2018-03-18 /pmc/articles/PMC5885386/ /pubmed/29515090 http://dx.doi.org/10.24272/j.issn.2095-8137.2018.025 Text en © 2018. Editorial Office of Zoological Research, Kunming Institute of Zoology, Chinese Academy of Sciences http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Article
Zhao, Feng
Lan, Xin-Qiang
Du, Yan
Chen, Pei-Yi
Zhao, Jiao
Zhao, Fang
Lee, Wen-Hui
Zhang, Yun
King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates
title King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates
title_full King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates
title_fullStr King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates
title_full_unstemmed King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates
title_short King cobra peptide OH-CATH30 as a potential candidate drug through clinic drug-resistant isolates
title_sort king cobra peptide oh-cath30 as a potential candidate drug through clinic drug-resistant isolates
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5885386/
https://www.ncbi.nlm.nih.gov/pubmed/29515090
http://dx.doi.org/10.24272/j.issn.2095-8137.2018.025
work_keys_str_mv AT zhaofeng kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates
AT lanxinqiang kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates
AT duyan kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates
AT chenpeiyi kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates
AT zhaojiao kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates
AT zhaofang kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates
AT leewenhui kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates
AT zhangyun kingcobrapeptideohcath30asapotentialcandidatedrugthroughclinicdrugresistantisolates