Detection by monoclonal antibodies of an early membrane protein induced by Epstein-Barr virus.
AUTOR(ES)
Balachandran, N
RESUMO
Two monoclonal antibodies, E8B3 and E8D2, were raised against Epstein-Barr virus (EBV)-producing cells and were shown to immunoprecipitate a protein with an approximate molecular weight of 105,000 (p105). The protein was detectable only in EBV-containing cells which were supporting the virus lytic cycle, and its synthesis increased after cells were induced with phorbol esters. The molecule was radiolabeled and immunoprecipitated from virus-producing cells that had been extrinsically labeled with 125I, and the antibodies E8B3 and E8D2 reacted in immunofluorescence assays with infected cells; the molecule was also associated with virion particles. Synthesis of p105 was not blocked by phosphonoacetic acid and could be induced in Raji cells by superinfection with virus derived from P3HR1 cells. These data support the conclusion that p105 is an EBV-specific early membrane protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=288902Documentos Relacionados
- Posttranslational processing of an Epstein-Barr virus-encoded membrane protein expressed in cells transformed by Epstein-Barr virus.
- Clonal origins of lymphoproliferative disease induced by Epstein-Barr virus.
- Immunobiochemical characterization with monoclonal antibodies of Epstein-Barr virus-associated early antigens in chemically induced cells.
- Production and characterization of monoclonal antibodies against the Epstein-Barr virus membrane antigen.
- Proteins of Epstein-Barr virus. I. Analysis of the polypeptides of purified enveloped Epstein-Barr virus.