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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1988-6-21
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/G protein, vesicular stomatitis...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Core Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
164
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
458-66
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3369089-Capsid,
pubmed-meshheading:3369089-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3369089-Glycoside Hydrolases,
pubmed-meshheading:3369089-Membrane Glycoproteins,
pubmed-meshheading:3369089-Molecular Weight,
pubmed-meshheading:3369089-Neuraminidase,
pubmed-meshheading:3369089-Respiratory Syncytial Viruses,
pubmed-meshheading:3369089-Structure-Activity Relationship,
pubmed-meshheading:3369089-Tunicamycin,
pubmed-meshheading:3369089-Viral Core Proteins,
pubmed-meshheading:3369089-Viral Envelope Proteins,
pubmed-meshheading:3369089-Viral Fusion Proteins,
pubmed-meshheading:3369089-Viral Matrix Proteins,
pubmed-meshheading:3369089-Viral Proteins,
pubmed-meshheading:3369089-Virus Replication
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pubmed:year |
1988
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pubmed:articleTitle |
Role of oligosaccharides in the structure and function of respiratory syncytial virus glycoproteins.
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pubmed:affiliation |
Department of Molecular Virology, James N. Gamble Institute of Medical Research, Cincinnati, Ohio 45219.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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