The 1A protein of respiratory syncytial virus is an integral membrane protein present as multiple, structurally distinct species
Abstract
The respiratory syncytial virus (RSV) 1A protein was previously identified as a 7.5-kilodalton (kDa) nonglycosylated species that, on the basis of its predicted sequence determined from the sequence of its mRNA, contains a hydrophobic central domain that was suggestive of membrane interaction. Here, …
Keywords
National Center for Biotechnology Information
NCBI
NLM
MEDLINE
pubmed abstract
nih
national institutes of health
national library of medicine
amino acid sequence
Antigens
Viral / analysis
Molecular Sequence Data
fluorescent antibody technique
r a olmsted
p l collins
molecular weight
pmid:2649692
pmc250617
doi:10.1128/jvi.63.5.2019-2029.1989
surface / analysis
glycoside hydrolases / pharmacology
membrane glycoproteins / analysis*
precipitin tests
protein processing
post-translational / drug effects
respiratory syncytial viruses / analysis*
tunicamycin / pharmacology
viral envelope proteins / analysis*
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114635
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