title: Polarized budding of vesicular stomatitis and influenza virus from cultured human and bovine retinal pigment epithelium.
abstract: The retinal pigment epithelium (RPE) is able to perform a variety of functions because of its high degree of plasma membrane polarity. Some aspects of this polarity such as the localization of the majority of Na-K ATPase to the apical membrane distinguish the RPE from kidney cells and most other transporting epithelia. The polarized budding of enveloped viruses such as vesicular stomatitis and influenza from the basolateral and apical membrane, respectively, has been used to study mechanisms underlying the domain-specific sorting of membrane proteins in cultured epithelial cell lines. These processes also serve as a useful index of the degree of polarization in epithelial cell cultures. Viral budding from apical and basolateral RPE membranes was used in this study to determine whether the sorting of viral envelope membrane proteins by the RPE is reversed in polarity from that of kidney cells and, if so, whether this might predict a fundamental difference in membrane protein sorting for RPE. The results clearly indicate that the polarity of viral membrane sorting and subsequent viral budding is the same in RPE as in other polarized epithelial cell lines examined to date.
authors.affiliation: Department of Anatomy and Cell Biology, School of Medicine, University of California, Los Angeles 90024.
authors.forename: D
authors.initials: D
authors.lastname: Bok
authors.forename: W
authors.initials: W
authors.lastname: O'Day
authors.forename: E
authors.initials: E
authors.lastname: Rodriguez-Boulan
mesh_terms: D000818:Animals; D002417:Cattle; D002478:Cells, Cultured; D005333:Fetus; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D009980:Influenza A virus / Q000378:metabolism*; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D010857:Pigment Epithelium of Eye / Q000378:metabolism* / Q000382:microbiology / Q000648:ultrastructure; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism
chemical_list: D014764:Viral Proteins; D019204:GTP-Binding Proteins