Role of oligosaccharides in the structure and function of respiratory syncytial virus glycoproteins
Identifieur interne : 001534 ( Main/Exploration ); précédent : 001533; suivant : 001535Role of oligosaccharides in the structure and function of respiratory syncytial virus glycoproteins
Auteurs : Dennis M. Lambert [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1988.
English descriptors
- Teeft :
- Carbohydrate, Digestion, Endo, Endoglycosidase, Endoglycosidase digestion, Endoglycosidase treatments, Endoglycosidases, Enzyme preparations, Fernie, Fusion protein, Glycoprotein, Glycosylated, Glycosylation, Gruber, Hep2, Hep2 cell monolayers, Infectivity, Lambert, Levine, Molecular weight, Molecular weights, Monoclonal, Monoclonal antibody, Neuraminidase, Oligosaccharide, Oligosaccharide side chains, Polyacrylamide, Polypeptide, Protease activity, Protein, Protein bands, Respiratory syncytial virus, Room temperature, Smaller species, Syncytial, Tunicamycin, Unglycosylated, Unglycosylated species, Untreated, Viral, Viral glycoproteins, Virion, Virion proteins, Virus, Virus glycoproteins, Virus infectivity, Western blot analysis, Western blots.
Abstract
Abstract: 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 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-α-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.
Url:
DOI: 10.1016/0042-6822(88)90560-0
Affiliations:
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<term>Endoglycosidase treatments</term>
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<term>Molecular weights</term>
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<front><div type="abstract" xml:lang="en">Abstract: 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 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-α-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.</div>
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