Summary for 1FJ1
| Entry DOI | 10.2210/pdb1fj1/pdb |
| Related | 1OSP |
| Descriptor | HYBRIDOMA ANTIBODY LA2 (LIGHT CHAIN), HYBRIDOMA ANTIBODY LA2 (HEAVY CHAIN), OUTER SURFACE PROTEIN A, ... (4 entities in total) |
| Functional Keywords | ospa, lyme disease, antibody fab fragment, neutralizing epitope, immune system |
| Biological source | Borrelia burgdorferi More |
| Total number of polymer chains | 6 |
| Total formula weight | 147839.11 |
| Authors | Ding, W.,Lawson, C.L. (deposition date: 2000-08-07, release date: 2000-10-11, Last modification date: 2023-08-09) |
| Primary citation | Ding, W.,Huang, X.,Yang, X.,Dunn, J.J.,Luft, B.J.,Koide, S.,Lawson, C.L. Structural identification of a key protective B-cell epitope in Lyme disease antigen OspA. J.Mol.Biol., 302:1153-1164, 2000 Cited by PubMed Abstract: Outer surface protein A (OspA) is a major lipoprotein of the Borrelia burgdorferi spirochete, the causative agent of Lyme disease. Vaccination with OspA generates an immune response that can prevent bacterial transmission to a mammalian host during the attachment of an infected tick. However, the protective capacity of immune sera cannot be predicted by measuring total anti-OspA antibody. The murine monoclonal antibody LA-2 defines an important protective B-cell epitope of OspA against which protective sera have strong levels of reactivity. We have now mapped the LA-2 epitope of OspA using both NMR chemical-shift perturbation measurements in solution and X-ray crystal structure determination. LA-2 recognizes the three surface-exposed loops of the C-terminal domain of OspA that are on the tip of the elongated molecule most distant from the lipid-modified N terminus. The structure suggests that the natural variation at OspA sequence position 208 in the first loop is a major limiting factor for antibody cross-reactivity between different Lyme disease-causing Borrelia strains. The unusual Fab-dominated lattice of the crystal also permits a rare view of antigen flexibility within an antigen:antibody complex. These results provide a rationale for improvements in OspA-based vaccines and suggest possible designs for more direct tests of antibody protective levels in vaccinated individuals. PubMed: 11183781DOI: 10.1006/jmbi.2000.4119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.68 Å) |
Structure validation
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