Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues

Chiara Zurzolo, Claudio Polistina, Marco Saini, Raffaele Gentile, Luigi Aloj, Giovanni Migliaccio, Stefano Bonatti, Lucio Nitsch

Research output: Contribution to journalArticlepeer-review

Abstract

We compared the surface envelope glycoprotein distribution and the budding polarity of four RNA viruses in Fischer rat thyroid (FRT) cells and in CaCo-2 cells derived from a human colon carcinoma. Whereas both FRT and CaCo-2 cells sort similarly influenza hemagglutinin and vesicular stomatitis virus (VSV) G protein, respectively, to apical and basolateral membrane domains, they differ in their handling of two togaviruses, Sindbis and Semliki Forest virus (SFV). By conventional EM Sindbis virus and SFV were shown to bud apically in FRT cells and basolaterally in CaCo-2 cells. Consistent with this finding, the distribution of the p62/E2 envelope glycoprotein of SFV, assayed by immunoelectronmicroscopy and by domain-selective surface biotinylation was predominantly apical on FRT cells and basolateral on CaCo-2 cells. We conclude that a given virus and its envelope glycoprotein can be delivered to opposite membrane domains in epithelial cells derived from different tissues. The tissue specificity in the polarity of virus budding and viral envelope glycoprotein distribution indicate that the sorting machinery varies considerably between different epithelial cell types.

Original languageEnglish
Pages (from-to)551-564
Number of pages14
JournalJournal of Cell Biology
Volume117
Issue number3
Publication statusPublished - May 1992

ASJC Scopus subject areas

  • Cell Biology

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