Suppression of glycoprotein formation of Semliki Forest, influenza, and avian sarcoma virus by tunicamycin.
AUTOR(ES)
Schwarz, R T
RESUMO
Tunicamycin, a new antibiotic, halts the formation of physical particles of Semliki forest and fowl plague virus, whereas avian oncornavirus particles which show a reduction in infectivity and do not contain detectable labeled glycoprotein are released in the presence of the drug. In Semliki forest virus-infected cells only the protein moieties of the glycoproteins could be labeled. In cells infected with fowl plague and avian sarcoma virus neither intact glycoproteins nor their protein moieties could be detected. By using a protease inhibitor (N-alpha-p-tosyl-L-lysin chloromethyl ketone, TLCK) it could be shown, however, that the carbohydrate-free hemagglutinin precursor of influenza virus is synthesized but is presumably degraded by intracellular proteases in the absence of TLCK as a consequence of the lack of carbohydrate.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=354919Documentos Relacionados
- Biosynthesis of an unglycosylated envelope glycoprotein of Rous sarcoma virus in the presence of tunicamycin.
- Modification of Epstein-Barr virus replication by tunicamycin.
- Evidence for role of glycoprotein carbohydrates in membrane transport: specific inhibition by tunicamycin.
- Assembly of viral membranes: maturation of the vesicular stomatitis virus glycoprotein in the presence of tunicamycin.
- Trypanosoma brucei brucei: inhibition of glycosylation of the major variable surface coat glycoprotein by tunicamycin.
