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dc.contributor.authorDay, ChristopherJ
dc.contributor.authorPaton, Adrienne W
dc.contributor.authorHarvey, Richard M
dc.contributor.authorHartley-Tassell, Lauren E
dc.contributor.authorSeib, Kate L
dc.contributor.authorTiralongo, Joe
dc.contributor.authorBovin, Nicolai
dc.contributor.authorSavino, Silvana
dc.contributor.authorMasignani, Vega
dc.contributor.authorPaton, James C
dc.contributor.authorJennings, Michael P
dc.date.accessioned2018-03-13T04:40:23Z
dc.date.available2018-03-13T04:40:23Z
dc.date.issued2017
dc.identifier.issn2045-2322
dc.identifier.doi10.1038/s41598-017-17850-9
dc.identifier.urihttp://hdl.handle.net/10072/371105
dc.description.abstractStreptococcus 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.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofpagefrom17784-1
dc.relation.ispartofpageto17784-6
dc.relation.ispartofjournalScientific Reports
dc.relation.ispartofvolume7
dc.relation.urihttp://purl.org/au-research/grants/NHMRC/APP1045235
dc.relation.grantIDAPP1045235
dc.relation.fundersNHMRC
dc.subject.fieldofresearchOther chemical sciences not elsewhere classified
dc.subject.fieldofresearchcode349999
dc.titleLectin activity of the pneumococcal pilin proteins
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/
dc.description.versionVersion of Record (VoR)
gro.facultyGriffith Sciences, School of Natural Sciences
gro.rights.copyright© The Author(s) 2017. 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/.
gro.hasfulltextFull Text
gro.griffith.authorJennings, Michael P.
gro.griffith.authorHartley-Tassell, Lauren E.
gro.griffith.authorDay, Christopher J.
gro.griffith.authorTiralongo, Joe
gro.griffith.authorSeib, Kate


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