ArticleJournal of proteome research2014
Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission.
Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- Immunogenic recombinant Mayaro virus-like particles present natively assembled glycoprotein.NPJ vaccines · 2024Article
- Negative-mode mass spectrometry in the analysis of invertebrate, fungal, and protist N-glycans.Mass spectrometry reviews · 2022Review
- Formation and fragmentation of doubly and triply charged ions in the negative ion spectra of neutral N-glycans from viral and other glycoproteins.Analytical and bioanalytical chemistry · 2021Article
- The Structural Biology of Eastern Equine Encephalitis Virus, an Emerging Viral Threat.Pathogens (Basel, Switzerland) · 2021Review
- A Roadmap for the Molecular Farming of Viral Glycoprotein Vaccines: Engineering Glycosylation and Glycosylation-Directed Folding.Frontiers in plant science · 2020Review
- Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019Review
- Cryo-EM Structures of Eastern Equine Encephalitis Virus Reveal Mechanisms of Virus Disassembly and Antibody Neutralization.Cell reports · 2018Article
- Applications of Ion Mobility-Mass Spectrometry in Carbohydrate Chemistry and Glycobiology.Molecules (Basel, Switzerland) · 2018Review
- Structure of the Lassa virus glycan shield provides a model for immunological resistance.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural Studies of Fucosylated N-Glycans by Ion Mobility Mass Spectrometry and Collision-Induced Fragmentation of Negative Ions.Journal of the American Society for Mass Spectrometry · 2018Article
- Article
- Shielding and activation of a viral membrane fusion protein.Nature communications · 2018Article
- Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Travelling-wave ion mobility and negative ion fragmentation of high-mannose N-glycans.Journal of mass spectrometry : JMS · 2016Article
- The fucomic potential of mosquitoes: Fucosylated N-glycan epitopes and their cognate fucosyltransferases.Insect biochemistry and molecular biology · 2016Article
- Ion Mobility Mass Spectrometry for Ion Recovery and Clean-Up of MS and MS/MS Spectra Obtained from Low Abundance Viral Samples.Journal of the American Society for Mass Spectrometry · 2015Article
- Targeted release and fractionation reveal glucuronylated and sulphated N- and O-glycans in larvae of dipteran insects.Journal of proteomics · 2015Article
- Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies.Nature communications · 2015Article
- Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design.Current opinion in virology · 2015Review
- Determination of N-linked Glycosylation in Viral Glycoproteins by Negative Ion Mass Spectrometry and Ion Mobility.Methods in molecular biology (Clifton, N.J.) · 2015Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
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.
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