Cargando…
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...
Autores principales: | , , , , , , , , |
---|---|
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 |
_version_ | 1784658352245047296 |
---|---|
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. |
format | Online Article Text |
id | pubmed-8877177 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT zhangwei discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT xuxiaohang discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT zhangjun discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT yeting discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT zhouqiao discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT xuying discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT liwenyi discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT huzhangli discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite AT shangchenjing discoveryandcharacterizationofanewcrustinantimicrobialpeptidefromamphibalanusamphitrite |