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Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium

BACKGROUND: Streptococcus suis is a zoonotic pathogen, causing meningitis and septicemia. We previously demonstrated that the gastrointestinal tract (GIT) is an entry site for zoonotic S. suis infection. Here we studied the contribution of Streptococcal adhesin Protein (SadP) to host-pathogen intera...

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Autores principales: Ferrando, Maria Laura, Willemse, Niels, Zaccaria, Edoardo, Pannekoek, Yvonne, van der Ende, Arie, Schultsz, Constance
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5391093/
https://www.ncbi.nlm.nih.gov/pubmed/28407026
http://dx.doi.org/10.1371/journal.pone.0175639
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author Ferrando, Maria Laura
Willemse, Niels
Zaccaria, Edoardo
Pannekoek, Yvonne
van der Ende, Arie
Schultsz, Constance
author_facet Ferrando, Maria Laura
Willemse, Niels
Zaccaria, Edoardo
Pannekoek, Yvonne
van der Ende, Arie
Schultsz, Constance
author_sort Ferrando, Maria Laura
collection PubMed
description BACKGROUND: Streptococcus suis is a zoonotic pathogen, causing meningitis and septicemia. We previously demonstrated that the gastrointestinal tract (GIT) is an entry site for zoonotic S. suis infection. Here we studied the contribution of Streptococcal adhesin Protein (SadP) to host-pathogen interaction at GIT level. METHODS: SadP expression in presence of Intestinal Epithelial Cells (IEC) was compared with expression of other virulence factors by measuring transcript levels using quantitative Real Time PCR (qRT-PCR). SadP variants were identified by phylogenetic analysis of complete DNA sequences. The interaction of SadP knockout and complementation mutants with IEC was tested in vitro. RESULTS: Expression of sadP was significantly increased in presence of IEC. Sequence analysis of 116 invasive strains revealed five SadP sequence variants, correlating with genotype. SadP1, present in zoonotic isolates of clonal complex 1, contributed to binding to both human and porcine IEC and translocation across human IEC. Antibodies against the globotriaosylceramide Gb3/CD77 receptor significantly inhibited adhesion to human IEC. CONCLUSION: SadP is involved in the host-pathogen interaction in the GIT. Differences between SadP variants may determine different affinities to the Gb3/CD77 host-receptor, contributing to variation in adhesion capacity to host IEC and thus to S. suis zoonotic potential.
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spelling pubmed-53910932017-05-03 Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium Ferrando, Maria Laura Willemse, Niels Zaccaria, Edoardo Pannekoek, Yvonne van der Ende, Arie Schultsz, Constance PLoS One Research Article BACKGROUND: Streptococcus suis is a zoonotic pathogen, causing meningitis and septicemia. We previously demonstrated that the gastrointestinal tract (GIT) is an entry site for zoonotic S. suis infection. Here we studied the contribution of Streptococcal adhesin Protein (SadP) to host-pathogen interaction at GIT level. METHODS: SadP expression in presence of Intestinal Epithelial Cells (IEC) was compared with expression of other virulence factors by measuring transcript levels using quantitative Real Time PCR (qRT-PCR). SadP variants were identified by phylogenetic analysis of complete DNA sequences. The interaction of SadP knockout and complementation mutants with IEC was tested in vitro. RESULTS: Expression of sadP was significantly increased in presence of IEC. Sequence analysis of 116 invasive strains revealed five SadP sequence variants, correlating with genotype. SadP1, present in zoonotic isolates of clonal complex 1, contributed to binding to both human and porcine IEC and translocation across human IEC. Antibodies against the globotriaosylceramide Gb3/CD77 receptor significantly inhibited adhesion to human IEC. CONCLUSION: SadP is involved in the host-pathogen interaction in the GIT. Differences between SadP variants may determine different affinities to the Gb3/CD77 host-receptor, contributing to variation in adhesion capacity to host IEC and thus to S. suis zoonotic potential. Public Library of Science 2017-04-13 /pmc/articles/PMC5391093/ /pubmed/28407026 http://dx.doi.org/10.1371/journal.pone.0175639 Text en © 2017 Ferrando 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 (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Ferrando, Maria Laura
Willemse, Niels
Zaccaria, Edoardo
Pannekoek, Yvonne
van der Ende, Arie
Schultsz, Constance
Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium
title Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium
title_full Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium
title_fullStr Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium
title_full_unstemmed Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium
title_short Streptococcal Adhesin P (SadP) contributes to Streptococcus suis adhesion to the human intestinal epithelium
title_sort streptococcal adhesin p (sadp) contributes to streptococcus suis adhesion to the human intestinal epithelium
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5391093/
https://www.ncbi.nlm.nih.gov/pubmed/28407026
http://dx.doi.org/10.1371/journal.pone.0175639
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