Antigenic determinants reacting with rheumatoid factor: Epitopes with different primary sequences share similar conformation

Molecular Immunology

Volumn 34, Issue 7, 1997, Pages 543-556

  Williams Jr , Ralph C ^a   Malone, Christine C ^a   Kolaskar, A S ^b   Kulkarni Kale, Urmila ^b  

^a UNIVERSITY OF FLORIDA   (United States)

^b UNIVERSITY OF PUNE   (India)

Author keywords

Antigen conformation; Antigenic epitopes; Rheumatoid factor

Indexed keywords

AUTOANTIBODY; BETA 2 MICROGLOBULIN; EPITOPE; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; RABBIT ANTISERUM; RHEUMATOID FACTOR;

AMINO ACID SEQUENCE; ARTICLE; CONFORMATION; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; MOLECULAR MODEL; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; BINDING, COMPETITIVE; EPITOPES; EPITOPES, B-LYMPHOCYTE; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RABBITS; RHEUMATOID FACTOR;

ORYCTOLAGUS CUNICULUS;

EID: 0343907869     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(97)00024-2     Document Type: Article

References (29)

1. Amit A. G., Mariuzza R. A., Phillips S. E. V. and Poljak R. J. (1986) Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 233, 747-753.
2. Appel J. R., Pinilla C., Niman H. and Houghten R. (1990) Elucidation of discontinuous linear determinants in peptides. J. Immunol. 144, 976-983.
3. Bodmer W. F. (1972) Evolutionary significance of the HL-A system. Nature 237, 139-145.
4. Das M. K. and Lindstrom J. (1991) Epitope mapping of antibodies to acetylcholine receptor α-subunits using peptides synthesized on polypropylene pegs. Biochemistry 30, 2470-2477.
5. Diesenhoffer J., Colman P. M. and Epp O., Huber R. (1976) A crystallographic structural studies of a human Fc fragment II complete model based on a Fourier map at 3.5 Å resolution Z. Physiol. Chem. 357, 1421-1434.
6. Diesenhoffer J., Jones T. A., Huber R., Sjodahl J. and Sjoquist J. (1978) Crystallization, crystal structure analysis and atomic model of the complex formed by a human Fc fragment and fragment B of protein A Staphylococcus aureus. Hoppe-Seyler's Z. Physiol. Chem. 359, 975-985.
7. Doolittle R. F., Hunkapiller M. W., Hood L. E., Devare S. G., Robbins K. C., Aronson S. A. and Antoniades H. N. (1983) Simian sarcoma virus one gene, v-sis is derived from the gene or (genes) encoding a platelet-derived growth factor. Science 221, 275-277.
8. Franklin E. C., Holman H. R., Muller-Eberhard H. J. and Kunkel H. G. (1957) An unusual protein component of high molecular weight in the serum of patients with rheumatoid arthritis. J. exp. Med. 105, 425-538.
9. Fudenberg H. H. and Kunkel H. G. (1961) Specificity of the reaction between rheumatoid factors and gamma globulin. J. exp. Med. 114, 257-278.
10. Kabsch W. and Sanders C. (1984) On the use of sequence homologies to predict protein structure: identical penta peptides can have completely different conformations. Proc. natn. Acad. Sci. U.S.A. 81, 1075-1078.
11. Kolaskar A. S. and Kulkarni-Kale U. (1992) Sequence alignment approach to pick up conformationally similar protein fragments. J. molec. Biol. 223, 1053-1061.
12. Kolaskar A. S. and Ramabrahmam V. (1981) Conformational similarity among amino acid residues: I. Analysis of crystal structure data. Int. J. Biol. Macromol. 3, 171-178.
13. Kolaskar A. S. and Ramabrahmam V. (1984) Are secondary structures secondary?. Int. J. Peptide and Protein Res. 24, 392-401.
14. Kunkel H. G., Franklin E. C., Muller-Eberhard H. J. (1959) Studies on the isolation and characterization of the "rheumatoid factor". J. clin. Invest. 38, 424-434.
15. Laurents D. V., Subbiah S. and Levitt M. (1994) Different protein sequences can give rise to highly similar folds through different stabilizing interactions. Prot. Sci. 3, 1938-1944.
16. Novotny J., Handschumacher M. and Haber E. (1986) Location of antigenic epitopes on antibody molecules. J. molec. Biol. 189, 715-721.
17. Padlan E. A., Silverton E. W., Streiff S., Cohen G. H., Smith-Gill S. J. and Davies D. R. (1989) Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fablysozyme complex. Proc. natn. Acad. Sci U.S.A. 86, 5938-5942.
18. 2-microglobulin: a free immunoglobulin domain. Proc. natn. Acad. Sci. U.S.A. 69, 1697-1701.
19. Peterson C., Malone C. C., Williams R. C. Jr. (1995) Rheumatoid factor reactive sites on CH3 established by overlapping 7-mer peptide epitope analysis. Molec. Immunol. 32, 57-75.
20. Quaratino S., Thorpe C. J., Travers P. J. and Londei M. (1995) Similar antigenic surfaces, rather than sequence homology, dictate T-cell epitope molecular mimicry. Proc. natn. Acad. Sci. U.S.A. 92, 10398-10402.
21. Saper M. A., Bjorkman P. J. and Wiley D. C. (1991) Refined structure of the human histocompatability antigen HLA-A2 at 2.6 Å resolution. J. molec. Biol. 219, 277-319.
22. Waterfield M. D., Scrace G. T., Whittle N., Stroobant P., Johnson A., Wasteson A., Westermark B., Heldin C. H., Huang J. S. and Deuel T. F. (1983) Platelet-derived growth factor is structurally related to the putative transforming protein p28 of simian sarcoma virus. Nature 304, 35-39.
23. Williams R. C. Jr. (1996) Autoimmune mechanisms involved in pathogenesis of rheumatoid arthritis. Adv. Dent. Res. 10, 47-51.
24. Williams R. C. Jr., Kievit E., Tsuchiya N., Malone C. and Huff-Fletcher L. (1992) Differential mapping of Fcγ-binding and monoclonal antibody-reactive epitopes on gE, the Fc γ-binding glycoprotein of herpes simplex virus type 1. J. Immunol. 149, 2415-2427.
25. 2m reacting with monoclonal antibodies. J. Lab. Clin. Med. 121, 805-820.
26. Williams R. C. Jr. and Malone C. C. (1994) Rheumatoid Factor Reactive sites on CH2 established by analysis of overlapping peptides of primary sequence. Scand. J. Immunol. 40, 443-456.
27. 2-microglobulin. Arthritis Rheum. 36, 916-926.
28. 2 microglobulin. J. Immunol. 149, 1104-1113.
29. Wucherpfennig K. W. and Strominger J. L. (1995) Molecular mimicry in T cell-mediated autoimmunity: viral peptides activate human T cell clones specific for myelin basic protein. Cell 80, 695-705.