JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schwarz, R. T.
Right arrow Articles by Klenk, H.-D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schwarz, R. T.
Right arrow Articles by Klenk, H.-D.

Next Article 

J Virol. 1974 November; 14(5): 1023-1034
Copyright © 1974 American Society for Microbiology. All Rights Reserved.

Inhibition of Glycosylation of the Influenza Virus Hemagglutinin

Ralph T. Schwarz and Hans-Dieter Klenk

Institut für Virologie, Justus Liebig-Universität, Geissen, Germany

ABSTRACT

D-Glucosamine and 2-deoxy-D-glucose interfere with the biosynthesis of the hemagglutinin glycoproteins. With increasing inhibitor concentrations a progressive decrease in size of the precursor HA and the cleavage products, HA1 and HA2 can be observed. The shift in molecular weight is paralleled by a decrease of the carbohydrate content. This was shown by labeling studies with radioactive sugars which revealed that the inhibitors block the incorporation into glycoproteins, whereas they have no or only slight effects on the uptake and activation of sugars. Under conditions of maximal inhibition, the hemagglutinin proteins lack all or most of their carbohydrates. These findings indicate that the inhibitory effect of D-glucosamine and 2-deoxy-D-glucose is due to an impairment of glycosylation. When glycosylation is inhibited, the precursor polypeptide is synthesized at normal rates. Its cleavage products, however, are very heterogeneous. This suggests that carbohydrate protects the hemagglutinin from proteolytic degradation.


J Virol. 1974 November; 14(5): 1023-1034
Copyright © 1974 American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 1974 by the American Society for Microbiology. All rights reserved.