Cargando…
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...
Autores principales: | , , , , , |
---|---|
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 |
_version_ | 1783229211837726720 |
---|---|
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. |
format | Online Article Text |
id | pubmed-5391093 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT ferrandomarialaura streptococcaladhesinpsadpcontributestostreptococcussuisadhesiontothehumanintestinalepithelium AT willemseniels streptococcaladhesinpsadpcontributestostreptococcussuisadhesiontothehumanintestinalepithelium AT zaccariaedoardo streptococcaladhesinpsadpcontributestostreptococcussuisadhesiontothehumanintestinalepithelium AT pannekoekyvonne streptococcaladhesinpsadpcontributestostreptococcussuisadhesiontothehumanintestinalepithelium AT vanderendearie streptococcaladhesinpsadpcontributestostreptococcussuisadhesiontothehumanintestinalepithelium AT schultszconstance streptococcaladhesinpsadpcontributestostreptococcussuisadhesiontothehumanintestinalepithelium |