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Virology. 2011 Jan 20;409(2):223-33. doi: 10.1016/j.virol.2010.10.011. Epub 2010 Nov 5.

Glycosylation modulates arenavirus glycoprotein expression and function.

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  • 1University of California, Irvine, Department of Molecular Biology and Biochemistry & Division of Infectious Disease, 3205 McGaugh Hall, Irvine, CA 92697-3900, USA. cbonhomm@uci.edu

Abstract

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.

Copyright © 2010 Elsevier Inc. All rights reserved.

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