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Lectin activity of the pneumococcal pilin proteins

Streptococcus pneumoniae is a leading cause of morbidity and mortality globally. The Pilus-1 proteins, RrgA, RrgB and RrgC of S. pneumoniae have been previously assessed for their role in infection, invasive disease and as possible vaccine candidates. In this study we have investigated the glycan bi...

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Autores principales: Day, Christopher J., Paton, Adrienne W., Harvey, Richard M., Hartley-Tassell, Lauren E., Seib, Kate L., Tiralongo, Joe, Bovin, Nicolai, Savino, Silvana, Masignani, Vega, Paton, James C., Jennings, Michael P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5736695/
https://www.ncbi.nlm.nih.gov/pubmed/29259314
http://dx.doi.org/10.1038/s41598-017-17850-9
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author Day, Christopher J.
Paton, Adrienne W.
Harvey, Richard M.
Hartley-Tassell, Lauren E.
Seib, Kate L.
Tiralongo, Joe
Bovin, Nicolai
Savino, Silvana
Masignani, Vega
Paton, James C.
Jennings, Michael P.
author_facet Day, Christopher J.
Paton, Adrienne W.
Harvey, Richard M.
Hartley-Tassell, Lauren E.
Seib, Kate L.
Tiralongo, Joe
Bovin, Nicolai
Savino, Silvana
Masignani, Vega
Paton, James C.
Jennings, Michael P.
author_sort Day, Christopher J.
collection PubMed
description Streptococcus pneumoniae is a leading cause of morbidity and mortality globally. The Pilus-1 proteins, RrgA, RrgB and RrgC of S. pneumoniae have been previously assessed for their role in infection, invasive disease and as possible vaccine candidates. In this study we have investigated the glycan binding repertoire of all three Pilus-1 proteins, identifying that the tip adhesin RrgA has the broadest glycan recognition of the three proteins, binding to maltose/cellobiose, α/β linked galactose and blood group A and H antigens. RrgB only bound mannose, while RrgC bound a subset of glycans also recognized by RrgA. Adherence of S. pneumoniae TIGR4 to epithelial cells was tested using four of the oligosaccharides identified through the glycan array analysis as competitive inhibitors. The blood group H trisaccharide provided the best blocking of S. pneumoniae TIGR4 adherence. Adherence is the first step in disease, and host glycoconjugates are a common target for many adhesins. This study has identified Pilus-1 proteins as new lectins involved in the targeting of host glycosylation by S. pneumoniae.
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spelling pubmed-57366952017-12-21 Lectin activity of the pneumococcal pilin proteins Day, Christopher J. Paton, Adrienne W. Harvey, Richard M. Hartley-Tassell, Lauren E. Seib, Kate L. Tiralongo, Joe Bovin, Nicolai Savino, Silvana Masignani, Vega Paton, James C. Jennings, Michael P. Sci Rep Article Streptococcus pneumoniae is a leading cause of morbidity and mortality globally. The Pilus-1 proteins, RrgA, RrgB and RrgC of S. pneumoniae have been previously assessed for their role in infection, invasive disease and as possible vaccine candidates. In this study we have investigated the glycan binding repertoire of all three Pilus-1 proteins, identifying that the tip adhesin RrgA has the broadest glycan recognition of the three proteins, binding to maltose/cellobiose, α/β linked galactose and blood group A and H antigens. RrgB only bound mannose, while RrgC bound a subset of glycans also recognized by RrgA. Adherence of S. pneumoniae TIGR4 to epithelial cells was tested using four of the oligosaccharides identified through the glycan array analysis as competitive inhibitors. The blood group H trisaccharide provided the best blocking of S. pneumoniae TIGR4 adherence. Adherence is the first step in disease, and host glycoconjugates are a common target for many adhesins. This study has identified Pilus-1 proteins as new lectins involved in the targeting of host glycosylation by S. pneumoniae. Nature Publishing Group UK 2017-12-19 /pmc/articles/PMC5736695/ /pubmed/29259314 http://dx.doi.org/10.1038/s41598-017-17850-9 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Day, Christopher J.
Paton, Adrienne W.
Harvey, Richard M.
Hartley-Tassell, Lauren E.
Seib, Kate L.
Tiralongo, Joe
Bovin, Nicolai
Savino, Silvana
Masignani, Vega
Paton, James C.
Jennings, Michael P.
Lectin activity of the pneumococcal pilin proteins
title Lectin activity of the pneumococcal pilin proteins
title_full Lectin activity of the pneumococcal pilin proteins
title_fullStr Lectin activity of the pneumococcal pilin proteins
title_full_unstemmed Lectin activity of the pneumococcal pilin proteins
title_short Lectin activity of the pneumococcal pilin proteins
title_sort lectin activity of the pneumococcal pilin proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5736695/
https://www.ncbi.nlm.nih.gov/pubmed/29259314
http://dx.doi.org/10.1038/s41598-017-17850-9
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