Unusual heterogeneity in the glycosylation of the G protein of the Hazelhurst strain of vesicular stomatitis virus
| Autor: | Lawrence A. Hunt, Sandra K. Davidson, Daniel Golemboski |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Glycosylation
G protein Biophysics Oligosaccharides Biology Vesicular stomatitis Indiana virus Kidney Biochemistry Chromatography Affinity Cell Line Viral Proteins chemistry.chemical_compound Species Specificity Viral Envelope Proteins Affinity chromatography Cricetinae Protein A/G Baby hamster kidney cell Animals Molecular Biology Membrane Glycoproteins Glycopeptides Vesiculovirus biology.organism_classification Molecular biology Sialic acid chemistry Vesicular stomatitis virus biology.protein Protein Processing Post-Translational |
| Zdroj: | Archives of Biochemistry and Biophysics. 226:347-356 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(83)90301-6 |
| Popis: | The asparagine-linked oligosaccharides of the G protein of the Hazelhurst subtype of the New Jersey serotype of vesicular stomatitis virus (VSV) have been compared with the oligosaccharides from the G protein of the well-characterized Indiana serotype of VSV, with baby hamster kidney cells in monolayer culture as the host for both viruses. [3H]Glucosamine- and [3H]mannose-labeled glycopeptides from the G protein of purified virus were analyzed by the combined techniques of endo-beta-N-acetylglucosaminidase H (ENDO-H) digestion, concanavalin A and lentil lectin affinity chromatography, and Bio-Gel P-4 chromatography. Although almost all of the Indiana G protein oligosaccharides were acidic-type structures, as expected from previous studies; the Hazelhurst G protein contained a mixture of acidic-type, hybrid-type containing sialic acid, and neutral-type (predominantly Man5-6GlcNAc2-Asn) structures. The vast majority of acidic-type oligosaccharides from both the Hazelhurst and Indiana G proteins were diantennary structures, with less than half containing fucose linked to the innermost N-acetylglucosamine. Additional analysis of the Hazelhurst G protein by ENDO-H digestion and gel electrophoresis suggested that some of the mature G polypeptides contained acidic-type structures at both glycosylation sites, whereas the remainder contained an ENDO-H-resistant, acidic-type structure at one site and an ENDO-H-sensitive, hybrid- or neutral-type structure at the other site. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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