Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/110438
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Type: Journal article
Title: Lectin activity of the pneumococcal pilin proteins
Author: Day, C.
Paton, A.
Harvey, R.
Hartley-Tassell, L.
Seib, K.
Tiralongo, J.
Bovin, N.
Savino, S.
Masignani, V.
Paton, J.
Jennings, M.
Citation: Scientific Reports, 2017; 7(1):17784-1-17784-6
Publisher: Nature Publishing Group
Issue Date: 2017
ISSN: 2045-2322
2045-2322
Statement of
Responsibility: 
Christopher J. Day, Adrienne W. Paton, Richard M. Harvey, Lauren E. Hartley-Tassell, Kate L. Seib, Joe Tiralongo, Nicolai Bovin, Silvana Savino, Vega Masignani, James C. Paton and Michael P. Jennings
Abstract: 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.
Keywords: Cell Line, Tumor; Fimbriae, Bacterial; Epithelial Cells; Humans; Streptococcus pneumoniae; Galactose; Cellobiose; Maltose; Bacterial Proteins; Fimbriae Proteins; Lectins; Virulence Factors; Antigens, Bacterial; Protein Binding; A549 Cells
Rights: © 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/.
RMID: 0030079431
DOI: 10.1038/s41598-017-17850-9
Appears in Collections:Molecular and Biomedical Science publications

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