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Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission
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Crispin, Max, Harvey, David J., Bitto, David, Bonomelli, Camille, Edgeworth, Matthew, Scrivens, James H., Huiskonen, Juha T. and Bowden, Thomas A. (2014) Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission. Journal of proteome research, Volume 13 (Number 3). pp. 1702-1712. doi:10.1021/pr401162k ISSN 1535-3893.
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Official URL: http://dx.doi.org/10.1021/pr401162k
Abstract
Cross-species viral transmission subjects parent and progeny alphaviruses to differential post-translational processing of viral envelope glycoproteins. Alphavirus biogenesis has been extensively studied, and the Semliki Forest virus E1 and E2 glycoproteins have been shown to exhibit differing degrees of processing of N-linked glycans. However the composition of these glycans, including that arising from different host cells, has not been determined. Here we determined the chemical composition of the glycans from the prototypic alphavirus, Semliki Forest virus, propagated in both arthropod and rodent cell lines, by using ion-mobility mass spectrometry and collision-induced dissociation analysis. We observe that both the membrane-proximal E1 fusion glycoprotein and the protruding E2 attachment glycoprotein display heterogeneous glycosylation that contains N-linked glycans exhibiting both limited and extensive processing. However, E1 contained predominantly highly processed glycans dependent on the host cell, with rodent and mosquito-derived E1 exhibiting complex-type and paucimannose-type glycosylation, respectively. In contrast, the protruding E2 attachment glycoprotein primarily contained conserved under-processed oligomannose-type structures when produced in both rodent and mosquito cell lines. It is likely that glycan processing of E2 is structurally restricted by steric-hindrance imposed by local viral protein structure. This contrasts E1, which presents glycans characteristic of the host cell and is accessible to enzymes. We integrated our findings with previous cryo-electron microscopy and crystallographic analyses to produce a detailed model of the glycosylated mature virion surface. Taken together, these data reveal the degree to which virally encoded protein structure and cellular processing enzymes shape the virion glycome during interspecies transmission of Semliki Forest virus.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QR Microbiology | ||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||
Library of Congress Subject Headings (LCSH): | Virus diseases -- Transmission, Glycoproteins | ||||||||
Journal or Publication Title: | Journal of proteome research | ||||||||
Publisher: | American Chemical Society | ||||||||
ISSN: | 1535-3893 | ||||||||
Official Date: | 7 March 2014 | ||||||||
Dates: |
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Volume: | Volume 13 | ||||||||
Number: | Number 3 | ||||||||
Number of Pages: | 11 | ||||||||
Page Range: | pp. 1702-1712 | ||||||||
DOI: | 10.1021/pr401162k | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||
Date of first compliant deposit: | 29 December 2015 | ||||||||
Date of first compliant Open Access: | 29 December 2015 | ||||||||
Funder: | Wellcome Trust (London, England), Suomen Akatemia [Academy of Finland], Medical Research Council (Great Britain) (MRC) | ||||||||
Grant number: | 090532/Z/09/Z (WT), 089026/Z/09/Z (WT), 130750 (SA), 218080 (SA), MR/L009528/1 (MRC) |
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