Glycosylation modulates arenavirus glycoprotein expression and function

Journal Article · Thu Jan 20 04:00:00 EST 2011 · Virology

DOI:https://doi.org/10.1016/j.virol.2010.10.011· OSTI ID:21486914

The glycoprotein of lymphocytic choriomeningitis virus (LCMV) contains nine potential N-linked glycosylation sites. We investigated the function of these N-glycosylations by using alanine-scanning mutagenesis. All the available sites were occupied on GP1 and two of three on GP2. N-linked glycan mutations at positions 87 and 97 on GP1 resulted in reduction of expression and absence of cleavage and were necessary for downstream functions, as confirmed by the loss of GP-mediated fusion activity with T87A and S97A mutants. In contrast, T234A and E379N/A381T mutants impaired GP-mediated cell fusion without altered expression or processing. Infectivity via virus-like particles required glycans and a cleaved glycoprotein. Glycosylation at the first site within GP2, not normally utilized by LCMV, exhibited increased VLP infectivity. We also confirmed the role of the N-linked glycan at position 173 in the masking of the neutralizing epitope GP-1D. Taken together, our results indicated a strong relationship between fusion and infectivity.

• OSTI ID: 21486914
• Journal Information: Virology, Journal Name: Virology Journal Issue: 2 Vol. 409; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ALANINES
AMINO ACIDS
CARBOHYDRATES
CARBOXYLIC ACIDS
GLYCOPROTEINS
INFECTIVITY
MICROORGANISMS
MUTAGENESIS
MUTANTS
MUTATIONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PROTEINS
SACCHARIDES
VIRUSES