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Published on: May 4, 2012
DNA hydrolysis by monoclonal autoantibody BV 04-01
L S Rodkey1, G Gololobov, C A Rumbley
1Department of Pathology and Laboratory Medicine, University of Texas-Houston, Medical School, 7225-0708, USA.
Applied Biochemistry and Biotechnology
|May 29, 2000
Summary
Monoclonal antibody BV 04-01, in the presence of Mg2+, effectively catalyzed DNA hydrolysis. This catalytic activity, observed in various antibody forms, suggests a potential germline-encoded function for antibodies.
Area of Science:
- Biochemistry
- Immunology
- Molecular Biology
Background:
- Autoantibodies can exhibit catalytic activity, a function often overlooked.
- Monoclonal antibody BV 04-01 is known to interact with DNA.
Purpose of the Study:
- To investigate the catalytic hydrolysis of DNA by monoclonal antibody BV 04-01.
- To elucidate the mechanism and structural basis of this antibody-mediated DNA cleavage.
Main Methods:
- Assessing DNA hydrolysis by BV 04-01 IgG, Fab, and single-chain-antibody (SCA) proteins in the presence of Mg2+.
- Analyzing cleavage specificity on single-stranded (ssDNA) and double-stranded DNA (dsDNA), including specific sequences.
- Utilizing X-ray crystallography data and kinetic analysis of wild-type and mutant SCA to model the catalytic site.
Main Results:
- BV 04-01 demonstrated catalytic hydrolysis of both ssDNA and dsDNA, with preference for C-rich and CG-rich regions, respectively.
- Structural modeling indicated that catalytic activity involves conformational strain induction and Mg2+ coordination at the active site.
- The catalytic site appeared to be germline-encoded, suggesting an inherent antibody function.
Conclusions:
- Monoclonal antibody BV 04-01 catalyzes DNA hydrolysis via a mechanism involving conformational strain and metal ion coordination.
- The germline origin of the catalytic site suggests that catalytic activity is an intrinsic, albeit understudied, property of some antibodies.
