Polarity of influenza and vesicular stomatitis virus maturation in MDCK cells: Lack of a requirement for glycosylation of viral glycoproteins

M. G. Roth, J. P. Fitzpatrick, R. W. Compans

Research output: Contribution to journalArticle

56 Scopus citations

Abstract

We have investigated whether glycosylation of membrane glycoproteins is a determinant of the site of maturation of enveloped viruses in Madin-Darby canine kidney (MDCK) cells. In MDCK cell monolayers, vesicular stomatitis virus buds exclusively from the basal or lateral plasma membranes and contains a sialylated glycoprotein, whereas influenza virus buds exclusively from the apical plasma membrane and lacks neuraminic acid. In order to study the possible relationship between glycosylation of viral glycoproteins and the budding site, infected MDCK cells were treated with tunicamycin at a concentration that completely inhibits glycosylation of viral glycoproteins and the site of virus maturation was examined by electron microscopy. When tunicamycin-treated monolayers were compared to controls, the polarity in the maturation sites of both viruses was maintained. These results indicate that glycosylation of viral glycoproteins is not required for the determination of the cellular maturation site of these enveloped viruses.

Original languageEnglish (US)
Pages (from-to)6430-6434
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number12
DOIs
StatePublished - Jan 1 1979

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Polarity of influenza and vesicular stomatitis virus maturation in MDCK cells: Lack of a requirement for glycosylation of viral glycoproteins'. Together they form a unique fingerprint.

  • Cite this