title: Bovine papillomavirus type 1 alters the processing of host glucose- and calcium-modulated endoplasmic reticulum proteins.
abstract: We have previously characterized five proteins induced by the presence of the E2 open reading frame (ORF) region of bovine papillomavirus type 1 (BPV-1) in C127 mouse fibroblasts (R. M. Levenson, U. G. Brinckmann, M. K. O'Banion, E. J. Androphy, J. T. Schiller, F. Tabatabai, L. P. Turek, K. Neary, M. T. Chin, T. R. Broker, L. T. Chow, and D. A. Young, Virology 172:170-179, 1989). By specific immunoprecipitation, we now find that one of the papillomavirus-associated proteins (pvp1) is a highly glycosylated form of glucose-regulated protein 100 (grp100), a major constituent of the endoplasmic reticulum. A second set of pvps (2, 3, and 4) are shown to be related precursors of another protein already present in C127 cells (protein B). Based on their induction by the calcium ionophore A23187 and their positions on giant two-dimensional gels, we have tentatively identified pvp2, -3, and -4 and B as forms of calcium-regulated protein 55, another constituent of the endoplasmic reticulum (D. R. J. Macer and G. L. E. Koch, J. Cell Sci. 91:61-70, 1988). The mechanism by which BPV-1 brings about these changes is not yet defined; however, it is unlikely to involve calcium level perturbations or transformation per se, since ionophore treatment changes other proteins in C127 cells not seen with BPV and the papillomavirus-associated proteins are found in nontransformed cells harboring the E2 ORF region. Furthermore, the BPV changes are not associated with increased grp mRNA levels, as occurs in ionophore-treated cells. Rather, it appears that BPV-1 somehow retards the normal processing of these resident endoplasmic reticulum proteins that are believed to serve as critical regulators of host protein processing and assembly.
authors.affiliation: Department of Medicine, University of Rochester School of Medicine and Dentistry, New York 14642.
authors.forename: M K
authors.initials: MK
authors.lastname: O'Banion
authors.forename: D A
authors.initials: DA
authors.lastname: Young
mesh_terms: D000818:Animals; D015152:Blotting, Northern; D052688:Bovine papillomavirus 1 / Q000502:physiology*; D000001:Calcimycin / Q000494:pharmacology; D002118:Calcium / Q000502:physiology; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D002478:Cells, Cultured; D015180:Electrophoresis, Gel, Two-Dimensional; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D000091342:Endoplasmic Reticulum Chaperone BiP; D015870:Gene Expression; D005947:Glucose / Q000502:physiology; D006031:Glycosylation; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D018832:Molecular Chaperones; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000235:genetics; D014412:Tumor Virus Infections / Q000378:metabolism*; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D002352:Carrier Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D012333:RNA, Messenger; C069182:glucose-regulated protein 100; C018551:glucose-regulated proteins; D014415:Tunicamycin; D000001:Calcimycin; D005947:Glucose; D002118:Calcium