Suppression of Glycoprotein Formation of Semliki Forest, Influenza, and Avian Sarcoma Virus by Tunicamycin

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1976 Sep 1

PMID 184299

Citations 71

Authors

R T Schwarz

J M Rohrschneider

M F Schmidt

Affiliations

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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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