Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: altered O-glycosylation in the presence of brefeldin A

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ID: 116754
1992
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Abstract
The post-translational maturation of the attachment G glycoprotein of human respiratory syncytial virus (RSV) was investigated. The G protein formed homo-oligomers which sedimented in sucrose gradients at the same rate as the fusion F protein tetramer. Oligomerization of the G protein was insensitiv …
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Authors Collins PL;Mottet G;;
Journal the journal of general virology
Year 1992
DOI
DOI not found
URL
http://www.ncbi.nlm.nih.gov/pubmed/1634876
Keywords
National Center for Biotechnology Information NCBI NLM MEDLINE humans pubmed abstract nih national institutes of health national library of medicine Antigens Molecular Sequence Data hn protein* viral envelope proteins viral proteins* respiratory syncytial viruses / metabolism* p l collins viral / biosynthesis* protein conformation respiratory syncytial viruses / drug effects protein processing carbohydrate sequence pmid:1634876 doi:10.1099/0022-1317-73-4-849 g mottet brefeldin a cyclopentanes / pharmacology* endoplasmic reticulum / metabolism exocytosis / physiology glycoproteins / biosynthesis* glycosylation golgi apparatus / metabolism lectins / metabolism n-acetylneuraminic acid oxidative phosphorylation palmitic acid palmitic acids / metabolism post-translational / drug effects* sialic acids / analysis

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