Comparison of N- and O-linked glycosylation patterns of ebolavirus glycoproteins

Amanda L Collar; Elizabeth C Clarke; Eduardo Anaya; Denise Merrill; Sarah Yarborough; Scott M Anthony; Jens H Kuhn; Christine Merle; Manfred Theisen; Steven B Bradfute

doi:10.1016/j.virol.2016.12.010

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Comparison of N- and O-linked glycosylation patterns of ebolavirus glycoproteins

Journal article

Open access

Peer reviewed

Comparison of N- and O-linked glycosylation patterns of ebolavirus glycoproteins

Amanda L Collar, Elizabeth C Clarke, Eduardo Anaya, Denise Merrill, Sarah Yarborough, Scott M Anthony, Jens H Kuhn, Christine Merle, Manfred Theisen and Steven B Bradfute

Virology (New York, N.Y.), Vol.502, pp.39-47

02/2017

DOI: 10.1016/j.virol.2016.12.010

PMID: 27984785

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Abstract

Ebolaviruses are emerging pathogens that cause severe and often fatal viral hemorrhagic fevers. Four distinct ebolaviruses are known to cause Ebola virus disease in humans. The ebolavirus envelope glycoprotein (GP ) is heavily glycosylated, but the precise glycosylation patterns of ebolaviruses are largely unknown. Here we demonstrate that approximately 50 different N-glycan structures are present in GP derived from the four pathogenic ebolaviruses, including high mannose, hybrid, and bi-, tri-, and tetra-antennary complex glycans with and without fucose and sialic acid. The overall N-glycan composition is similar between the different ebolavirus GP s. In contrast, the amount and type of O-glycan structures varies widely between ebolavirus GP s. Notably, this O-glycan dissimilarity is also present between two variants of Ebola virus, the original Yambuku variant and the Makona variant responsible for the most recent Western African epidemic. The data presented here should serve as the foundation for future ebolaviral entry and immunogenicity studies.

Amino Acid Motifs

Ebolavirus - chemistry

Ebolavirus - classification

Ebolavirus - genetics

Ebolavirus - metabolism

Glycosylation

Hemorrhagic Fever, Ebola - virology

Humans

Polysaccharides - metabolism

Viral Envelope Proteins - chemistry

Viral Envelope Proteins - genetics

Viral Envelope Proteins - metabolism

Details

Title: Subtitle: Comparison of N- and O-linked glycosylation patterns of ebolavirus glycoproteins
Creators: Amanda L Collar - University of New Mexico Hospital
Elizabeth C Clarke - University of New Mexico Hospital
Eduardo Anaya - University of New Mexico Hospital
Denise Merrill - University of New Mexico Hospital
Sarah Yarborough - University of New Mexico Hospital
Scott M Anthony - University of Iowa
Jens H Kuhn - National Institutes of Health
Christine Merle - Proteodynamics SARL, Riom, France.
Manfred Theisen - Proteodynamics SARL, Riom, France.
Steven B Bradfute - University of New Mexico Hospital
Resource Type: Journal article
Publication Details: Virology (New York, N.Y.), Vol.502, pp.39-47
DOI: 10.1016/j.virol.2016.12.010
PMID: 27984785
NLM abbreviation: Virology
ISSN: 0042-6822
eISSN: 1096-0341
Grant note: HHSN272200700016I / NIAID NIH HHS
Language: English
Date published: 02/2017
Academic Unit: Pathology
Record Identifier: 9984183985402771

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