Cargando…

A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease

BACKGROUND: The class Myxosporea encompasses about 2,400 species, most of which are parasites of fish and cause serious damage in aquaculture. Due to the concerns about food safety issues and limited knowledge of Myxozoa life cycle and fish immune system, no chemicals, antibiotics or immune modulato...

Descripción completa

Detalles Bibliográficos
Autores principales: Liu, Yuchun, Zhou, Zhigang, Miao, Wei, Zhang, Yuting, Cao, Yanan, He, Suxu, Bai, Dongqing, Yao, Bin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3242780/
https://www.ncbi.nlm.nih.gov/pubmed/22205999
http://dx.doi.org/10.1371/journal.pone.0029091
_version_ 1782219650997682176
author Liu, Yuchun
Zhou, Zhigang
Miao, Wei
Zhang, Yuting
Cao, Yanan
He, Suxu
Bai, Dongqing
Yao, Bin
author_facet Liu, Yuchun
Zhou, Zhigang
Miao, Wei
Zhang, Yuting
Cao, Yanan
He, Suxu
Bai, Dongqing
Yao, Bin
author_sort Liu, Yuchun
collection PubMed
description BACKGROUND: The class Myxosporea encompasses about 2,400 species, most of which are parasites of fish and cause serious damage in aquaculture. Due to the concerns about food safety issues and limited knowledge of Myxozoa life cycle and fish immune system, no chemicals, antibiotics or immune modulators are available to control myxozoa infection. Therefore, little can be done once Myxozoa establishment has occurred. METHODOLOGY/PRINCIPAL FINDINGS: In this paper we isolated Aeromonas veronii CD3 with significant myxospore shell valve-degrading ability from pond sediment. A 3,057-bp full-length chitinase gene was consequently cloned, and the corresponding mature, recombinant chitinase (ChiCD3) produced by Escherichia coli had substantial chitinase activity. The deduced sequence of ChiCD3 contained one catalytic domain, two chitin-binding domains, and one putative signal peptide. ChiCD3 had an optimal activity at 50°C and pH 6.0, and retained more than 50% of its optimal activity under warm water aquaculture conditions (∼30°C and pH ∼7.0). After incubation with ChiCD3, 38.0±4.8% of the myxospores had damaged shell valves, whereas myxospores incubated with commercially available chitinases remained intact. CONCLUSION/SIGNIFICANCE: This study reveals a new strategy to control myxozoan disease. ChiCD3 that has capacity to damage the shell valve of myxospores can be supplemented into fish feed and used to control Myxozoa-induced diseases specifically.
format Online
Article
Text
id pubmed-3242780
institution National Center for Biotechnology Information
language English
publishDate 2011
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-32427802011-12-28 A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease Liu, Yuchun Zhou, Zhigang Miao, Wei Zhang, Yuting Cao, Yanan He, Suxu Bai, Dongqing Yao, Bin PLoS One Research Article BACKGROUND: The class Myxosporea encompasses about 2,400 species, most of which are parasites of fish and cause serious damage in aquaculture. Due to the concerns about food safety issues and limited knowledge of Myxozoa life cycle and fish immune system, no chemicals, antibiotics or immune modulators are available to control myxozoa infection. Therefore, little can be done once Myxozoa establishment has occurred. METHODOLOGY/PRINCIPAL FINDINGS: In this paper we isolated Aeromonas veronii CD3 with significant myxospore shell valve-degrading ability from pond sediment. A 3,057-bp full-length chitinase gene was consequently cloned, and the corresponding mature, recombinant chitinase (ChiCD3) produced by Escherichia coli had substantial chitinase activity. The deduced sequence of ChiCD3 contained one catalytic domain, two chitin-binding domains, and one putative signal peptide. ChiCD3 had an optimal activity at 50°C and pH 6.0, and retained more than 50% of its optimal activity under warm water aquaculture conditions (∼30°C and pH ∼7.0). After incubation with ChiCD3, 38.0±4.8% of the myxospores had damaged shell valves, whereas myxospores incubated with commercially available chitinases remained intact. CONCLUSION/SIGNIFICANCE: This study reveals a new strategy to control myxozoan disease. ChiCD3 that has capacity to damage the shell valve of myxospores can be supplemented into fish feed and used to control Myxozoa-induced diseases specifically. Public Library of Science 2011-12-19 /pmc/articles/PMC3242780/ /pubmed/22205999 http://dx.doi.org/10.1371/journal.pone.0029091 Text en Liu et al. http://creativecommons.org/licenses/by/4.0/ 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 properly credited.
spellingShingle Research Article
Liu, Yuchun
Zhou, Zhigang
Miao, Wei
Zhang, Yuting
Cao, Yanan
He, Suxu
Bai, Dongqing
Yao, Bin
A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease
title A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease
title_full A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease
title_fullStr A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease
title_full_unstemmed A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease
title_short A Chitinase from Aeromonas veronii CD3 with the Potential to Control Myxozoan Disease
title_sort chitinase from aeromonas veronii cd3 with the potential to control myxozoan disease
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3242780/
https://www.ncbi.nlm.nih.gov/pubmed/22205999
http://dx.doi.org/10.1371/journal.pone.0029091
work_keys_str_mv AT liuyuchun achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT zhouzhigang achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT miaowei achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT zhangyuting achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT caoyanan achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT hesuxu achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT baidongqing achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT yaobin achitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT liuyuchun chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT zhouzhigang chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT miaowei chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT zhangyuting chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT caoyanan chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT hesuxu chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT baidongqing chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease
AT yaobin chitinasefromaeromonasveroniicd3withthepotentialtocontrolmyxozoandisease