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ABSTRACT: Background
N-linked glycosylation is a common posttranslational modification found on viral glycoproteins (GPs) and involved in promoting expression, cellular attachment, protection from proteases, and antibody evasion. The GP subunit GP2 of filoviruses contains 2 completely conserved N-linked glycosylation sites (NGSs) at N563 and N618, suggesting that they have been maintained through selective pressures.Methods
We assessed mutants lacking these glycans for expression and function to understand the role of these sites during Ebola virus entry.Results
Elimination of either GP2 glycan individually had a modest effect on GP expression and no impact on antibody neutralization of vesicular stomatitis virus pseudotyped with Ebola virus GP. However, loss of the N563 glyc
SUBMITTER: Lennemann NJ
PROVIDER: S-EPMC4564545 | biostudies-literature | 2015 Oct
REPOSITORIES: biostudies-literature