Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein.pdf

Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein.pdf

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Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein

VIROLOGY 222, 159–168 (1996) ARTICLE NO. 0406 Mutagenesis of the N-Linked Glycosylation Sites of the Yellow Fever Virus NS1 Protein: Effects on Virus Replication and Mouse Neurovirulence ISABELLA R. MUYLAERT,*,? THOMAS J. CHAMBERS,? RICARDO GALLER,§ and CHARLES M. RICE*,1 *Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110-1093; ?Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21004, Brazil; ?Department of Molecular Microbiology and Immunology, St. Louis University School of Medicine, St. Louis, Missouri 63104; and §Departamento de Bioqu?B mica e Biologia Molecular, Fundac?a?o Oswaldo Cruz, Rio de Janeiro 21040, Brazil Received April 14, 1996; accepted June 5, 1996 The flavivirus nonstructural glycoprotein NS1 is highly conserved and contains two N-linked glycosylation sites which are both utilized for addition of oligosaccharides during replication in cell culture. NS1 has been shown to contain epitopes for protective antibodies; however, its roles in virus replication and pathogenesis remain unknown. To study the function of NS1 during yellow fever virus replication, six mutant viruses which lack either one or both glycosylation sites and another one containing silent mutations at both sites were generated by site-directed mutagenesis. Mutants lacking the second glycosylation site and those bearing silent mutations were similar to the parental virus in their cell culture properties. Ablation of the first or both glycosylation sites generated mutants exhibiting small plaque phenotypes, decreased virus yields, reduced cytopathic effects, impaired NS1 secretion, and depressed RNA accumulation. In addition, mutants lacking the first or both glycosylation sites exhibited significant reduction in mouse neurovirulence after intracerebral inoculation. These defects appear to result from the lack of N-linked glycans rather than the introduction of deleterious amino acid substitutions

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