Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89123
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dc.contributor.authorPathak, Anujen
dc.contributor.authorBergstrand, Janen
dc.contributor.authorSender, Vickyen
dc.contributor.authorSpelmink, Lauraen
dc.contributor.authorAschtgen, Marie-Stephanieen
dc.contributor.authorMuschiol, Sandraen
dc.contributor.authorWidengren, Jerkeren
dc.contributor.authorHenriques-Normark, Birgittaen
dc.date.accessioned2018-09-24T06:02:18Zen
dc.date.accessioned2019-12-06T17:18:23Z-
dc.date.available2018-09-24T06:02:18Zen
dc.date.available2019-12-06T17:18:23Z-
dc.date.issued2018en
dc.identifier.citationPathak, A., Bergstrand, J., Sender, V., Spelmink, L., Aschtgen, M.-S., Muschiol, S., . . . Henriques-Normark, B. (2018). Factor H binding proteins protect division septa on encapsulated Streptococcus pneumoniae against complement C3b deposition and amplification. Nature Communications, 9(1), 3398-. doi:10.1038/s41467-018-05494-wen
dc.identifier.urihttps://hdl.handle.net/10356/89123-
dc.identifier.urihttp://hdl.handle.net/10220/46073en
dc.description.abstractStreptococcus pneumoniae evades C3-mediated opsonization and effector functions by expressing an immuno-protective polysaccharide capsule and Factor H (FH)-binding proteins. Here we use super-resolution microscopy, mutants and functional analysis to show how these two defense mechanisms are functionally and spatially coordinated on the bacterial cell surface. We show that the pneumococcal capsule is less abundant at the cell wall septum, providing C3/C3b entry to underlying nucleophilic targets. Evasion of C3b deposition at division septa and lateral amplification underneath the capsule requires localization of the FH-binding protein PspC at division sites. Most pneumococcal strains have one PspC protein, but successful lineages in colonization and disease may have two, PspC1 and PspC2, that we show affect virulence differently. We find that spatial localization of these FH-recruiting proteins relative to division septa and capsular layer is instrumental for pneumococci to resist complement-mediated opsonophagocytosis, formation of membrane-attack complexes, and for the function as adhesins.en
dc.format.extent16 p.en
dc.language.isoenen
dc.relation.ispartofseriesNature Communicationsen
dc.rights© 2018 The Author(s). 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/.en
dc.subjectC3b Depositionen
dc.subjectDRNTU::Science::Medicineen
dc.subjectBinding Proteinsen
dc.titleFactor H binding proteins protect division septa on encapsulated Streptococcus pneumoniae against complement C3b deposition and amplificationen
dc.typeJournal Articleen
dc.contributor.schoolLee Kong Chian School of Medicine (LKCMedicine)en
dc.contributor.researchSingapore Centre for Environmental Life Sciences and Engineeringen
dc.identifier.doi10.1038/s41467-018-05494-wen
dc.description.versionPublished versionen
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Appears in Collections:LKCMedicine Journal Articles

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