title: Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues.
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.
authors.affiliation: Centro di Endocrinologia ed Oncologia Sperimentale del Consiglio Nazionale delle Ricerche, Dipartimento di Biologia e Patologia Cellulare e Naples, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Zurzolo
authors.forename: C
authors.initials: C
authors.lastname: Polistina
authors.forename: M
authors.initials: M
authors.lastname: Saini
authors.forename: R
authors.initials: R
authors.lastname: Gentile
authors.forename: L
authors.initials: L
authors.lastname: Aloj
authors.forename: G
authors.initials: G
authors.lastname: Migliaccio
authors.forename: S
authors.initials: S
authors.lastname: Bonatti
authors.forename: L
authors.initials: L
authors.lastname: Nitsch
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000473:pathology* / Q000648:ultrastructure; D016764:Cell Polarity; D002478:Cells, Cultured; D003106:Colon / Q000166:cytology / Q000648:ultrastructure; D004848:Epithelium / Q000473:pathology / Q000648:ultrastructure; D019204:GTP-Binding Proteins / Q000302:isolation & purification; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000302:isolation & purification; D006801:Humans; D007150:Immunohistochemistry; D016253:Microscopy, Immunoelectron; D012328:RNA Viruses / Q000254:growth & development*; D051381:Rats; D012672:Semliki forest virus / Q000254:growth & development; D012845:Sindbis Virus / Q000254:growth & development; D013961:Thyroid Gland / Q000166:cytology / Q000648:ultrastructure; D014759:Viral Envelope Proteins / Q000302:isolation & purification / Q000378:metabolism*; D014777:Virus Diseases / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D014759:Viral Envelope Proteins; D019204:GTP-Binding Proteins