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. 1976 Sep;19(3):782–791. doi: 10.1128/jvi.19.3.782-791.1976

Suppression of glycoprotein formation of Semliki Forest, influenza, and avian sarcoma virus by tunicamycin.

R T Schwarz, J M Rohrschneider, M F Schmidt
PMCID: PMC354919  PMID: 184299

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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