The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity

Abstract Haemophilus parasuis is the causative agent of the Glässer’s disease (GD), one of the most important bacterial diseases that affect young pigs worldwide. GD prevention based on vaccination is a major concern due to the limited cross-protection conferred by the inactivated whole cell vaccine...

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Autores principales:	João Antônio Guizzo, Somshukla Chaudhuri, Simone Ramos Prigol, Rong-hua Yu, Cláudia Cerutti Dazzi, Natalia Balbinott, Gabriela Paraboni Frandoloso, Luiz Carlos Kreutz, Rafael Frandoloso, Anthony Bernard Schryvers
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6b04255a8fb44b9b8673082abe9e517c
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spelling	oai:doaj.org-article:6b04255a8fb44b9b8673082abe9e517c2021-12-02T12:32:09ZThe amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity10.1038/s41598-018-25685-12045-2322https://doaj.org/article/6b04255a8fb44b9b8673082abe9e517c2018-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-25685-1https://doaj.org/toc/2045-2322Abstract Haemophilus parasuis is the causative agent of the Glässer’s disease (GD), one of the most important bacterial diseases that affect young pigs worldwide. GD prevention based on vaccination is a major concern due to the limited cross-protection conferred by the inactivated whole cell vaccines used currently. In this study, vaccines based on two mutant recombinant proteins derived from transferrin binding protein B of H. parasuis (Y167A-TbpB and W176A-TbpB) were formulated and evaluated in terms of protection against lethal challenge using a serovar 7 (SV7) H. parasuis in a high susceptibility pig model. Our results showed that H. parasuis strain 174 (SV7) is highly virulent in conventional and colostrum-deprived pigs. The Y167A-TbpB and W176A-TbpB antigens were immunogenic in pigs, however, differences in terms of antigenicity and functional immune response were observed. In regard to protection, animals immunized with Y167A-TbpB antigen displayed 80% survival whereas the W176A-TbpB protein was not protective. In conjunction with previous studies, our results demonstrate, (a) the importance of testing engineered antigens in an in vivo pig challenge model, and, (b) that the Y167A-TbpB antigen is a promising antigen for developing a broad-spectrum vaccine against H. parasuis infection.João Antônio GuizzoSomshukla ChaudhuriSimone Ramos PrigolRong-hua YuCláudia Cerutti DazziNatalia BalbinottGabriela Paraboni FrandolosoLuiz Carlos KreutzRafael FrandolosoAnthony Bernard SchryversNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q João Antônio Guizzo Somshukla Chaudhuri Simone Ramos Prigol Rong-hua Yu Cláudia Cerutti Dazzi Natalia Balbinott Gabriela Paraboni Frandoloso Luiz Carlos Kreutz Rafael Frandoloso Anthony Bernard Schryvers The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity
description	Abstract Haemophilus parasuis is the causative agent of the Glässer’s disease (GD), one of the most important bacterial diseases that affect young pigs worldwide. GD prevention based on vaccination is a major concern due to the limited cross-protection conferred by the inactivated whole cell vaccines used currently. In this study, vaccines based on two mutant recombinant proteins derived from transferrin binding protein B of H. parasuis (Y167A-TbpB and W176A-TbpB) were formulated and evaluated in terms of protection against lethal challenge using a serovar 7 (SV7) H. parasuis in a high susceptibility pig model. Our results showed that H. parasuis strain 174 (SV7) is highly virulent in conventional and colostrum-deprived pigs. The Y167A-TbpB and W176A-TbpB antigens were immunogenic in pigs, however, differences in terms of antigenicity and functional immune response were observed. In regard to protection, animals immunized with Y167A-TbpB antigen displayed 80% survival whereas the W176A-TbpB protein was not protective. In conjunction with previous studies, our results demonstrate, (a) the importance of testing engineered antigens in an in vivo pig challenge model, and, (b) that the Y167A-TbpB antigen is a promising antigen for developing a broad-spectrum vaccine against H. parasuis infection.
format	article
author	João Antônio Guizzo Somshukla Chaudhuri Simone Ramos Prigol Rong-hua Yu Cláudia Cerutti Dazzi Natalia Balbinott Gabriela Paraboni Frandoloso Luiz Carlos Kreutz Rafael Frandoloso Anthony Bernard Schryvers
author_facet	João Antônio Guizzo Somshukla Chaudhuri Simone Ramos Prigol Rong-hua Yu Cláudia Cerutti Dazzi Natalia Balbinott Gabriela Paraboni Frandoloso Luiz Carlos Kreutz Rafael Frandoloso Anthony Bernard Schryvers
author_sort	João Antônio Guizzo
title	The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity
title_short	The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity
title_full	The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity
title_fullStr	The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity
title_full_unstemmed	The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity
title_sort	amino acid selected for generating mutant tbpb antigens defective in binding transferrin can compromise the in vivo protective capacity
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/6b04255a8fb44b9b8673082abe9e517c
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The amino acid selected for generating mutant TbpB antigens defective in binding transferrin can compromise the in vivo protective capacity

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