BAP37 and Prohibitin Are Specifically Recognized by an SV40 T Antigen Antibody

We have identified two cellular proteins that are specifically immunoprecipitated by an anti-SV40 T antigen monoclonal antibody. This antibody, PAb419, recognizes an epitope contained within a region of T antigen which we have recently demonstrated is required for the initiation of immortalization b...

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Bibliographic Details
Published in:Molecular cell biology research communications 2000-10, Vol.4 (4), p.219-223
Main Authors: Darmon, Alison J., Jat, Parmjit S.
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Antibodies, Monoclonal - metabolism
Antibody Specificity
Antigen-Antibody Complex - chemistry
Antigens, Polyomavirus Transforming - immunology
Antigens, Viral, Tumor - immunology
BAP37
Blotting, Western
Cell Line, Transformed - chemistry
E2F
Epitopes - immunology
Mice
p107
p130
Precipitin Tests
Prohibitin, SV40 large T antigen
Proteins - immunology
Repressor Proteins
retinoblastoma
Sequence Analysis, Protein
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Summary:We have identified two cellular proteins that are specifically immunoprecipitated by an anti-SV40 T antigen monoclonal antibody. This antibody, PAb419, recognizes an epitope contained within a region of T antigen which we have recently demonstrated is required for the initiation of immortalization by SV40 T antigen, but is not essential for maintenance of the immortal state. The two proteins were identified as BAP37 and Prohibitin. Recent results suggest Prohibitin may enhance the transcriptional inactivation of E2F by the retinoblastoma family of pocket proteins (pRb, p107, p130). BAP37 and Prohibitin are specifically recognized by PAb419 and PAb210, another anti-SV40 T antigen monoclonal antibody, which has an overlapping epitope, but not by other anti-SV40 T antigen monoclonal antibodies, demonstrating the specificity of the interaction.
ISSN:1522-4724
1522-4732
DOI:10.1006/mcbr.2001.0281