Oligomerization and post-translational processing of glycoprotein G of human respiratory syncytial virus: altered O-glycosylation in the presence of brefeldin A
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 …
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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Citation
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116754
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116754
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