Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-6-21
pubmed:abstractText
The contribution of oligosaccharides to the structural and functional make-up of respiratory syncytial (RS) virus G and F proteins was investigated by observing the effects of various oligosaccharide-specific enzymes on their molecular size as well as on virus infectivity. The N-linked oligosaccharides of the F protein were completely removed by endoglycosidase F and N-glycanase. Addition of oligosaccharides to F protein during synthesis was completely inhibited by the drug tunicamycin (TM), an inhibitor of N-linked glycosylation. Glycosylation of the G protein was partially resistant to TM resulting in an 80-kDa form designated GTM. The G protein was estimated to contain approximately 3% N-linked and 55% O-linked carbohydrates, based on migration of G and GTM in polyacrylamide gels. Furthermore, treatment of detergent-extracted G protein with endoglycosidase F and endo-alpha-N-acetylgalactosaminidase, enzymes that specifically cleave N-linked and O-linked oligosaccharides, respectively, generated a variety of partially unglycosylated species, ranging in molecular weight from approximately 80 to 40 kDa. Virus infectivity was sensitive to limited removal of N-linked or O-linked oligosaccharides by endoglycosidases under conditions which did not greatly alter the molecular weight of the G protein. Thus, G and F protein oligosaccharides readily accessible to enzymatic removal are presumed to play an important role in the infectious process.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
164
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
458-66
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Role of oligosaccharides in the structure and function of respiratory syncytial virus glycoproteins.
pubmed:affiliation
Department of Molecular Virology, James N. Gamble Institute of Medical Research, Cincinnati, Ohio 45219.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't