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A murine monoclonal antibody recognising a single glycoprotein within a human cytomegalovirus virion envelope glycoprotein complex
Author(s) -
Law Katherine M.,
WiltonSmith Peter,
Farrar Graham H.
Publication year - 1985
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.1890170307
Subject(s) - monoclonal antibody , glycoprotein , immunoprecipitation , human cytomegalovirus , microbiology and biotechnology , viral envelope , virology , immunofluorescence , polyacrylamide gel electrophoresis , antigen , antibody , biology , gel electrophoresis , chemistry , virus , biochemistry , enzyme , immunology
Nonionic detergent solubilised polypeptides from highly purified human cytomegalovirus virions were used as immunogens to produce murine monoclonal antibody secreting hybridomas. One monoclonal antibody was shown, by immunoprecipitation followed by SDS‐polyacrylamide gel electrophoresis (SDSPAGE), to precipitate three glycoproteins with molecular weights 52, 95, and 130 (all × 10 3 ) and one minor component with a molecular weight of 50 × 10 3 . When virion envelope components were first separated by SDS‐PAGE and electrophoretically transferred to nitrocellulose membranes, this monoclonal antibody recognised two related components with molecular weights 50 and 52 (both × 10 3 ). Immunofluorescence studies suggested that these viral antigens were associated with membrane systems of virus‐infected cells and were particularly abundant late in infection.