| First Author | James M | Year | 1997 |
| Journal | Biochim Biophys Acta | Volume | 1360 |
| Issue | 2 | Pages | 169-76 |
| PubMed ID | 9128182 | Mgi Jnum | J:39783 |
| Mgi Id | MGI:87132 | Doi | 10.1016/s0925-4439(96)00076-2 |
| Citation | James M, et al. (1997) The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta 1360(2):169-76 |
| abstractText | The epitope recognised by the anti-dystrophin monoclonal antibodies MANDYS141 and MANDYS142 has been characterised using a phage display peptide library and a bacteriophage lambda cDNA library. Using a phage display library of random 15-mer peptides, the epitope recognised by the two antibodies was identified as EEXF. A lambda gt11 clone obtained by screening a human muscle cDNA library was shown to contain part of the out-of-frame human mitochondrial succinyl CoA synthetase (alpha-subunit) cDNA sequence which contains the sequence EEPL, suggesting a minimum requirement of EEXF/L for antibody binding. The sequence EEDF is located in the helical rod region of dystrophin and the N-terminal domain of alpha-actinin; this may explain why native dystrophin is not detected, since the alpha-helical, coiled-coil folding of the rod region of dystrophin may obscure the epitope in the native protein. The antibody cross-reaction between dystrophin and alpha-actinin is likely to be fortuitous and not due to any structural homology that exists between these two members of the spectrin superfamily. |
