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Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1

BACKGROUND: Actinobacillus pleuropneumoniae (APP) is one of the most important swine pathogens worldwide. Identification and characterization of novel antigenic APP vaccine candidates are underway. In the present study, we use an immunoproteomic approach to identify APP protein antigens that may eli...

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Autores principales: Zhang, Wei, Shao, Jing, Liu, Guangjin, Tang, Fang, Lu, Yan, Zhai, Zhipeng, Wang, Yang, Wu, Zongfu, Yao, Huochun, Lu, Chengping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3148531/
https://www.ncbi.nlm.nih.gov/pubmed/21703014
http://dx.doi.org/10.1186/1477-5956-9-32
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author Zhang, Wei
Shao, Jing
Liu, Guangjin
Tang, Fang
Lu, Yan
Zhai, Zhipeng
Wang, Yang
Wu, Zongfu
Yao, Huochun
Lu, Chengping
author_facet Zhang, Wei
Shao, Jing
Liu, Guangjin
Tang, Fang
Lu, Yan
Zhai, Zhipeng
Wang, Yang
Wu, Zongfu
Yao, Huochun
Lu, Chengping
author_sort Zhang, Wei
collection PubMed
description BACKGROUND: Actinobacillus pleuropneumoniae (APP) is one of the most important swine pathogens worldwide. Identification and characterization of novel antigenic APP vaccine candidates are underway. In the present study, we use an immunoproteomic approach to identify APP protein antigens that may elicit an immune response in serotype 1 naturally infected swine and serotype 1 virulent strain S259-immunized rabbits. RESULTS: Proteins from total cell lysates of serotype 1 APP were separated by two-dimensional electrophoresis (2DE). Western blot analysis revealed 21 immunoreactive protein spots separated in the pH 4-7 range and 4 spots in the pH 7-11 range with the convalescent sera from swine; we found 5 immunoreactive protein spots that separated in the pH 4-7 range and 2 in the pH 7-11 range with hyperimmune sera from S259-immunized rabbits. The proteins included the known antigens ApxIIA, protective surface antigen D15, outer membrane proteins P5, subunit NqrA. The remaining antigens are being reported as immunoreactive proteins in APP for the first time, to our knowledge. CONCLUSIONS: We identified a total of 42 immunoreactive proteins of the APP serotype 1 virulent strain S259 which represented 32 different proteins, including some novel immunoreactive factors which could be researched as vaccine candidates.
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spelling pubmed-31485312011-08-03 Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1 Zhang, Wei Shao, Jing Liu, Guangjin Tang, Fang Lu, Yan Zhai, Zhipeng Wang, Yang Wu, Zongfu Yao, Huochun Lu, Chengping Proteome Sci Research BACKGROUND: Actinobacillus pleuropneumoniae (APP) is one of the most important swine pathogens worldwide. Identification and characterization of novel antigenic APP vaccine candidates are underway. In the present study, we use an immunoproteomic approach to identify APP protein antigens that may elicit an immune response in serotype 1 naturally infected swine and serotype 1 virulent strain S259-immunized rabbits. RESULTS: Proteins from total cell lysates of serotype 1 APP were separated by two-dimensional electrophoresis (2DE). Western blot analysis revealed 21 immunoreactive protein spots separated in the pH 4-7 range and 4 spots in the pH 7-11 range with the convalescent sera from swine; we found 5 immunoreactive protein spots that separated in the pH 4-7 range and 2 in the pH 7-11 range with hyperimmune sera from S259-immunized rabbits. The proteins included the known antigens ApxIIA, protective surface antigen D15, outer membrane proteins P5, subunit NqrA. The remaining antigens are being reported as immunoreactive proteins in APP for the first time, to our knowledge. CONCLUSIONS: We identified a total of 42 immunoreactive proteins of the APP serotype 1 virulent strain S259 which represented 32 different proteins, including some novel immunoreactive factors which could be researched as vaccine candidates. BioMed Central 2011-06-26 /pmc/articles/PMC3148531/ /pubmed/21703014 http://dx.doi.org/10.1186/1477-5956-9-32 Text en Copyright ©2011 Zhang et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Zhang, Wei
Shao, Jing
Liu, Guangjin
Tang, Fang
Lu, Yan
Zhai, Zhipeng
Wang, Yang
Wu, Zongfu
Yao, Huochun
Lu, Chengping
Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1
title Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1
title_full Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1
title_fullStr Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1
title_full_unstemmed Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1
title_short Immunoproteomic analysis of bacterial proteins of Actinobacillus pleuropneumoniae serotype 1
title_sort immunoproteomic analysis of bacterial proteins of actinobacillus pleuropneumoniae serotype 1
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3148531/
https://www.ncbi.nlm.nih.gov/pubmed/21703014
http://dx.doi.org/10.1186/1477-5956-9-32
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