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LCMV Glycosylation Modulates Viral Fitness and Cell Tropism
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LCMV Glycosylation Modulates Viral Fitness and Cell Tropism
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Journal Article
LCMV Glycosylation Modulates Viral Fitness and Cell Tropism
2013
Overview
The glycoprotein (GP) of arenaviruses is glycosylated at 11 conserved N-glycosylation sites. We constructed recombinant lymphocytic choriomeningitis virus (rLCMV) featuring either additions or deletions of these N-glycans to investigate their role in the viral life cycle. N-glycosylation at two sites, T87 and S97, were found to be necessary to rescue rLCMV. Three of nine successfully rescued mutants, S116A, T234A, and S373A, under selective pressures in either epithelial, neuronal, or macrophage cells reverted to WT sequence. Of the seven stable N-glycan deletion mutants, five of these led to altered viral fitness and cell tropism, assessed as growth in either mouse primary cortical neurons or bone marrow derived macrophages. These results demonstrate that the deletion of N-glycans in LCMV GP may confer an advantage to the virus for infection of neurons but a disadvantage in macrophages.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Biology
/ Deletion
/ Disease
/ Fitness
/ Glycan
/ HIV
/ Human immunodeficiency virus
/ Humans
/ Lymphocytic Choriomeningitis - veterinary
/ Lymphocytic Choriomeningitis - virology
/ Lymphocytic choriomeningitis virus - genetics
/ Lymphocytic choriomeningitis virus - growth & development
/ Lymphocytic choriomeningitis virus - metabolism
/ Medicine
/ Mice
/ Mutants
/ Mutation
/ Neurons
/ Polysaccharides - metabolism
/ Proteins
/ Tropism
/ Virology
/ Viruses
