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Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite

Crustins are an antimicrobial peptide (AMP) family that plays an important role in innate immunity in crustaceans. It is important to discover new AMPs from natural sources to expand the current database. Here, we identified and characterized a new crustin family member, named AaCrus1, from Amphibal...

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Autores principales: Zhang, Wei, Xu, Xiaohang, Zhang, Jun, Ye, Ting, Zhou, Qiao, Xu, Ying, Li, Wenyi, Hu, Zhangli, Shang, Chenjing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877177/
https://www.ncbi.nlm.nih.gov/pubmed/35214145
http://dx.doi.org/10.3390/pharmaceutics14020413
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author Zhang, Wei
Xu, Xiaohang
Zhang, Jun
Ye, Ting
Zhou, Qiao
Xu, Ying
Li, Wenyi
Hu, Zhangli
Shang, Chenjing
author_facet Zhang, Wei
Xu, Xiaohang
Zhang, Jun
Ye, Ting
Zhou, Qiao
Xu, Ying
Li, Wenyi
Hu, Zhangli
Shang, Chenjing
author_sort Zhang, Wei
collection PubMed
description Crustins are an antimicrobial peptide (AMP) family that plays an important role in innate immunity in crustaceans. It is important to discover new AMPs from natural sources to expand the current database. Here, we identified and characterized a new crustin family member, named AaCrus1, from Amphibalanus amphitrite. AaCrus1 shares high identity (48.10%) with PvCrus, a Type I crustin of Penaeus vannamei that possesses a whey acidic protein (WAP) domain. AaCrus1 contains 237 amino acids and eight cysteine residues forming conserved ‘four-disulfide core’ structure. Our recombinant AaCrus1 (rAaCrus 1) could inhibit the growth of two Gram-positive bacteria (Staphylococcus aureus, Bacillus sp. T2) and four Gram-negative bacteria (Vibrio parahaemolyticus, Vibrio harveyi, Vibrio anguillarum, Vibrio alginolyticus) with a minimum inhibitory concentration of 3.5–28 μM. It can further induce agglutination of both Gram-positive and Gram-negative bacteria. rAaCrus1 can bind to bacteria and damage bacterial cell membranes. Furthermore, rAaCrus1 disrupted biofilm development of S. aureus and V. parahaemolyticus. Our discovery and characterization of this new crustin can be further optimized as a good alternative to antibiotics.
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spelling pubmed-88771772022-02-26 Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite Zhang, Wei Xu, Xiaohang Zhang, Jun Ye, Ting Zhou, Qiao Xu, Ying Li, Wenyi Hu, Zhangli Shang, Chenjing Pharmaceutics Article Crustins are an antimicrobial peptide (AMP) family that plays an important role in innate immunity in crustaceans. It is important to discover new AMPs from natural sources to expand the current database. Here, we identified and characterized a new crustin family member, named AaCrus1, from Amphibalanus amphitrite. AaCrus1 shares high identity (48.10%) with PvCrus, a Type I crustin of Penaeus vannamei that possesses a whey acidic protein (WAP) domain. AaCrus1 contains 237 amino acids and eight cysteine residues forming conserved ‘four-disulfide core’ structure. Our recombinant AaCrus1 (rAaCrus 1) could inhibit the growth of two Gram-positive bacteria (Staphylococcus aureus, Bacillus sp. T2) and four Gram-negative bacteria (Vibrio parahaemolyticus, Vibrio harveyi, Vibrio anguillarum, Vibrio alginolyticus) with a minimum inhibitory concentration of 3.5–28 μM. It can further induce agglutination of both Gram-positive and Gram-negative bacteria. rAaCrus1 can bind to bacteria and damage bacterial cell membranes. Furthermore, rAaCrus1 disrupted biofilm development of S. aureus and V. parahaemolyticus. Our discovery and characterization of this new crustin can be further optimized as a good alternative to antibiotics. MDPI 2022-02-14 /pmc/articles/PMC8877177/ /pubmed/35214145 http://dx.doi.org/10.3390/pharmaceutics14020413 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Wei
Xu, Xiaohang
Zhang, Jun
Ye, Ting
Zhou, Qiao
Xu, Ying
Li, Wenyi
Hu, Zhangli
Shang, Chenjing
Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite
title Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite
title_full Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite
title_fullStr Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite
title_full_unstemmed Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite
title_short Discovery and Characterization of a New Crustin Antimicrobial Peptide from Amphibalanus amphitrite
title_sort discovery and characterization of a new crustin antimicrobial peptide from amphibalanus amphitrite
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877177/
https://www.ncbi.nlm.nih.gov/pubmed/35214145
http://dx.doi.org/10.3390/pharmaceutics14020413
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