Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.

<h4>Background</h4>There is a strong need for a recombinant subunit vaccine against fowl cholera. We used a reverse vaccinology approach to identify putative secreted or cell surface associated P. multocida proteins that may represent potential vaccine candidate antigens.<h4>Princi...

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Autores principales:	Tamás Hatfaludi, Keith Al-Hasani, Lan Gong, John D Boyce, Mark Ford, Ian W Wilkie, Noelene Quinsey, Michelle A Dunstone, David E Hoke, Ben Adler
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/484699b934ed4af39dccbfe03cc58423
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spelling	oai:doaj.org-article:484699b934ed4af39dccbfe03cc584232021-11-18T07:13:24ZScreening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.1932-620310.1371/journal.pone.0039973https://doaj.org/article/484699b934ed4af39dccbfe03cc584232012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22792202/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>There is a strong need for a recombinant subunit vaccine against fowl cholera. We used a reverse vaccinology approach to identify putative secreted or cell surface associated P. multocida proteins that may represent potential vaccine candidate antigens.<h4>Principal findings</h4>A high-throughput cloning and expression protocol was used to express and purify 71 recombinant proteins for vaccine trials. Of the 71 proteins tested, only one, PlpE in denatured insoluble form, protected chickens against fowl cholera challenge. PlpE also elicited comparable levels of protection in mice. PlpE was localized by immunofluorescence to the bacterial cell surface, consistent with its ability to elicit a protective immune response. To explore the role of PlpE during infection and immunity, a plpE mutant was generated. The plpE mutant strain retained full virulence for mice.<h4>Conclusion</h4>These studies show that PlpE is a surface exposed protein and was the only protein of 71 tested that was able to elicit a protective immune response. However, PlpE is not an essential virulence factor. This is the first report of a denatured recombinant protein stimulating protection against fowl cholera.Tamás HatfaludiKeith Al-HasaniLan GongJohn D BoyceMark FordIan W WilkieNoelene QuinseyMichelle A DunstoneDavid E HokeBen AdlerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e39973 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tamás Hatfaludi Keith Al-Hasani Lan Gong John D Boyce Mark Ford Ian W Wilkie Noelene Quinsey Michelle A Dunstone David E Hoke Ben Adler Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.
description	<h4>Background</h4>There is a strong need for a recombinant subunit vaccine against fowl cholera. We used a reverse vaccinology approach to identify putative secreted or cell surface associated P. multocida proteins that may represent potential vaccine candidate antigens.<h4>Principal findings</h4>A high-throughput cloning and expression protocol was used to express and purify 71 recombinant proteins for vaccine trials. Of the 71 proteins tested, only one, PlpE in denatured insoluble form, protected chickens against fowl cholera challenge. PlpE also elicited comparable levels of protection in mice. PlpE was localized by immunofluorescence to the bacterial cell surface, consistent with its ability to elicit a protective immune response. To explore the role of PlpE during infection and immunity, a plpE mutant was generated. The plpE mutant strain retained full virulence for mice.<h4>Conclusion</h4>These studies show that PlpE is a surface exposed protein and was the only protein of 71 tested that was able to elicit a protective immune response. However, PlpE is not an essential virulence factor. This is the first report of a denatured recombinant protein stimulating protection against fowl cholera.
format	article
author	Tamás Hatfaludi Keith Al-Hasani Lan Gong John D Boyce Mark Ford Ian W Wilkie Noelene Quinsey Michelle A Dunstone David E Hoke Ben Adler
author_facet	Tamás Hatfaludi Keith Al-Hasani Lan Gong John D Boyce Mark Ford Ian W Wilkie Noelene Quinsey Michelle A Dunstone David E Hoke Ben Adler
author_sort	Tamás Hatfaludi
title	Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.
title_short	Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.
title_full	Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.
title_fullStr	Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.
title_full_unstemmed	Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.
title_sort	screening of 71 p. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen plpe.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/484699b934ed4af39dccbfe03cc58423
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Screening of 71 P. multocida proteins for protective efficacy in a fowl cholera infection model and characterization of the protective antigen PlpE.

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