title: Comparison of N- and O-linked glycosylation patterns of ebolavirus glycoproteins.
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 (GP1,2) 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 GP1,2derived 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 GP1,2s. In contrast, the amount and type of O-glycan structures varies widely between ebolavirus GP1,2s. 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.
authors.affiliation: Center for Global Health, Division of Infectious Diseases, Department of Internal Medicine, University of New Mexico, Albuquerque, NM, USA.
authors.forename: Amanda L
authors.initials: AL
authors.lastname: Collar
authors.affiliation: Center for Global Health, Division of Infectious Diseases, Department of Internal Medicine, University of New Mexico, Albuquerque, NM, USA.
authors.forename: Elizabeth C
authors.initials: EC
authors.lastname: Clarke
authors.affiliation: Department of Pathology, University of New Mexico, Albuquerque, NM, USA.
authors.forename: Eduardo
authors.initials: E
authors.lastname: Anaya
authors.affiliation: Center for Global Health, Division of Infectious Diseases, Department of Internal Medicine, University of New Mexico, Albuquerque, NM, USA.
authors.forename: Denise
authors.initials: D
authors.lastname: Merrill
authors.affiliation: Undergraduate Pipeline Network, University of New Mexico, Albuquerque, NM, USA.
authors.forename: Sarah
authors.initials: S
authors.lastname: Yarborough
authors.affiliation: Department of Microbiology, University of Iowa, Iowa City, IA, USA.
authors.forename: Scott M
authors.initials: SM
authors.lastname: Anthony
authors.affiliation: Integrated Research Facility at Fort Detrick (IRF-Frederick), Division of Clinical Research (DCR), National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Fort Detrick, Frederick, MD, USA.
authors.forename: Jens H
authors.initials: JH
authors.lastname: Kuhn
authors.affiliation: Proteodynamics SARL, Riom, France.
authors.forename: Christine
authors.initials: C
authors.lastname: Merle
authors.affiliation: Proteodynamics SARL, Riom, France.
authors.forename: Manfred
authors.initials: M
authors.lastname: Theisen
authors.affiliation: Center for Global Health, Division of Infectious Diseases, Department of Internal Medicine, University of New Mexico, Albuquerque, NM, USA. Electronic address: sbradfute@salud.unm.edu.
authors.forename: Steven B
authors.initials: SB
authors.lastname: Bradfute
mesh_terms: D020816:Amino Acid Motifs; D029043:Ebolavirus / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D019142:Hemorrhagic Fever, Ebola / Q000821:virology*; D006801:Humans; D011134:Polysaccharides / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D011134:Polysaccharides; D014759:Viral Envelope Proteins; C113189:envelope glycoprotein, Ebola virus
keywords: Bundibugyo virus; Ebola virus; Ebolavirus; Filoviridae; Filovirus; Glycan; Glycoprotein; Glycosylation; Sudan virus; Taï Forest virus