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dc.contributor.authorSchwede, Angelaen
dc.contributor.authorMacleod, Oliviaen
dc.contributor.authorMacGregor, Paulaen
dc.contributor.authorCarrington, Marken
dc.date.accessioned2016-01-22T17:07:46Z
dc.date.available2016-01-22T17:07:46Z
dc.date.issued2015-12-31en
dc.identifier.citationPLOS Pathogens 2015, 11(12): e1005259. doi:10.1371/journal.ppat.1005259en
dc.identifier.issn1553-7366
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/253449
dc.description.abstractVariations on the statement “the variant surface glycoprotein (VSG) coat that covers the external face of the mammalian bloodstream form of Trypanosoma brucei acts a physical barrier” appear regularly in research articles and reviews. The concept of the impenetrable VSG coat is an attractive one, as it provides a clear model for understanding how a trypanosome population persists; each successive VSG protects the plasma membrane and is immunologically distinct from previous VSGs. What is the evidence that the VSG coat is an impenetrable barrier, and how do antibodies and other extracellular proteins interact with it? In this review, the nature of the extracellular surface of the bloodstream form trypanosome is described, and past experiments that investigated binding of antibodies and lectins to trypanosomes are analysed using knowledge of VSG sequence and structure that was unavailable when the experiments were performed. Epitopes for some VSG monoclonal antibodies are mapped as far as possible from previous experimental data, onto models of VSG structures. The binding of lectins to some, but not to other, VSGs is revisited with more recent knowledge of the location and nature of N-linked oligosaccharides. The conclusions are: (i) Much of the variation observed in earlier experiments can be explained by the identity of the individual VSGs. (ii) Much of an individual VSG is accessible to antibodies, and the barrier that prevents access to the cell surface is probably at the base of the VSG N-terminal domain, approximately 5 nm from the plasma membrane. This second conclusion highlights a gap in our understanding of how the VSG coat works, as several plasma membrane proteins with large extracellular domains are very unlikely to be hidden from host antibodies by VSG.
dc.description.sponsorshipThe authors’ lab is funded by the Wellcome Trust (093008/Z10/Z) and the Medical Research Council (MR/L008246/1). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
dc.languageEnglishen
dc.language.isoenen
dc.publisherPLOS
dc.rightsAttribution 2.0 UK: England & Wales*
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/uk/*
dc.titleHow Does the VSG Coat of Bloodstream Form African Trypanosomes Interact with External Proteins?en
dc.typeArticle
dc.description.versionThis is the final version of the article. It was first available from PLOS via http://dx.doi.org/10.1371/journal.ppat.1005259en
prism.numbere1005259en
prism.publicationDate2015en
prism.publicationNamePLOS Pathogensen
prism.volume11en
dc.rioxxterms.funderWellcome Trust
dc.rioxxterms.funderMRC
dc.rioxxterms.projectid093008/Z10/Z
dc.rioxxterms.projectidMR/L008246/1
rioxxterms.versionofrecord10.1371/journal.ppat.1005259en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-12-31en
dc.contributor.orcidMacleod, Olivia [0000-0002-5747-8019]
dc.contributor.orcidMacGregor, Paula [0000-0003-0919-3745]
dc.contributor.orcidCarrington, Mark [0000-0002-6435-7266]
dc.identifier.eissn1553-7374
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idMRC (MR/L008246/1)
pubs.funder-project-idWellcome Trust (093008/Z/10/Z)


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Attribution 2.0 UK: England & Wales
Except where otherwise noted, this item's licence is described as Attribution 2.0 UK: England & Wales