Synthesis and processing of glycoproteins of Varicella-Zoster virus (VZV) as studied with monoclonal antibodies to VZV antigens. 1983

T Okuno, and K Yamanishi, and K Shiraki, and M Takahashi

Varicella-Zoster virus (VZV) contains four major glycoproteins designated as gp 1(115K), gp 2(100-80K), gp 3(64K), and gp 5(55K) (K. Shiraki, T. Okuno, K. Yamanishi, and M. Takahashi, J. Gen. Virol. 61, 255-269, 1982). The present studies focused on the synthesis and processing of these glycoproteins using monoclonal antibodies. Twenty-seven hybridomas secreting monoclonal antibodies against VZV proteins have been established. The antibodies were characterized further by radioimmunoprecipitation with [35S]-methionine, [3H]glucosamine, [125I]labeled viral antigens followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Twelve clones of these hybridomas produced antibodies to glycosylated polypeptides of VZV, which could be classified into three groups on the basis of the electrophoretic patterns. The first group reacted specifically with polypeptides with apparent molecular weights of 94K and 83K (both presumed to correspond to gp 2) in infected cells, on the surface membrane of infected cells, and on the virions. The second group precipiated polypeptides with molecular weights of 94K, 83K, 55K (corresponding to gp 5) in infected cells, and 94K, 83K, 55K, 45K on the surface membrane of infected cells, and 94K, 83K, and 55K on the virions. Finally, the third group reacted with polypeptides with molecular weights of 116K, 106K, and 64K corresponding to gp 3) in infected cells, 64K on the surface membrane of infected cells, and on the virions. By pulse-chase experiments, antibodies from the former two groups precipitated new polypeptides with molecular weights of 75K and 49K, respectively, which were presumed to be precursor proteins. These data suggest that the precursor proteins of gp 2, gp 3, and gp 5 are synthesized in infected cells, glycosylated, and the product proteins are expressed on the surface membrane of infected cells as well as on the virions. It was also found that a glycoprotein of 45K detected in culture fluid of infected cells (K. Shiraki and M. Takahashi, J. Gen. Virol. 61, 271-275, 1982) was derived from the polypeptide with molecular weight of 55K (gp 5).

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D011498 Protein Precursors Precursors, Protein
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D006023 Glycoproteins Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins. C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
D006825 Hybridomas Cells artificially created by fusion of activated lymphocytes with neoplastic cells. The resulting hybrid cells are cloned and produce pure MONOCLONAL ANTIBODIES or T-cell products, identical to those produced by the immunologically competent parent cell. Hybridoma
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal
D000914 Antibodies, Viral Immunoglobulins produced in response to VIRAL ANTIGENS. Viral Antibodies

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