Studies on the development of the charge heterogeneity of the influenza virus glycoproteins.
The heterogeneity in charge of the influenza virus glycoproteins, hemagglutinin (HA) and neuraminidase (NA) is retained, when glycosylation is inhibited by tunicamycin (TM) or 2-deoxyglucose (2-dg). This is in contrast to the charge heterogeneity of the G protein of vesicular stomatitis virus (VSV), which is mainly due to heterogeneous sulfation of the carbohydrate side chains and therefore is abolished by the above mentioned inhibitors of glycosylation. Thus, the charge heterogeneity of influenza virus glycoproteins might be attributable to some as yet unidentified modifications of the polypeptide backbone.
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D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo; D003847:Deoxyglucose / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D009980:Influenza A virus / Q000032:analysis* / Q000201:enzymology / Q000378:metabolism; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008562:Membrane Glycoproteins; D009439:Neuraminidase; D014176:Protein Biosynthesis; D014415:Tunicamycin / Q000494:pharmacology; D014721:Vesicular stomatitis Indiana virus / Q000032:analysis; D014759:Viral Envelope Proteins; D014764:Viral Proteins
C028391:G protein, vesicular stomatitis virus; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D014415:Tunicamycin; D003847:Deoxyglucose; D009439:Neuraminidase