Studies on the Clonality of the Antibody Response to a Protein Epitope

  • Eli Benjamini
  • Matthew L. Andria
  • Soshana Levy
  • Cherry Y. Leung


During the past decade, great advances have been made in the synthesis and preparation of various formulations of compounds to be used as vaccines. Indeed, the field of “vaccinology” has experienced a dramatic surge. Yet, while many preparations, such as hepatis B immunogens, constitute effective vaccines, attempts to prepare effective vaccines against other diseases, such as malaria or AIDS, have encountered formidable difficulties.


Cell Clone Helper Cell Synthetic Analogue Fine Specificity Large Repertoire 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Akolar, P. N. Sikder, S. K., Bhattacharya, S. B., Liao, J., Gruezo, F., Morrison, S. L. and Kabat, E. A, 1987, Different V2 and VH germ line genes and used to produce similar confining sites with specificity for α(1––>6) dextran, J. Immunol., 138:4472.Google Scholar
  2. Benjamini, E, 1987, Expression of B- and T-cell responses to a defined epitope of a protein antigen in: Immunogenicity of Protein Antigens: Repertoire and Regulation, Vol. I, E. E. Sercarz and J. A. Berzofsky, Eds. CRC Press Inc. Boca Raton, Florida.Google Scholar
  3. Benjamini, E., Andria, M. L. , Estin, C. D., Norton, F. L. and Leung, C. Y, 1988, Studies on the clonality of the response to an epitope of a protein antigen: Randomness of activation of epitope recognizing clones and the development of clonal dominance, J. Immunol., 141:55.PubMedGoogle Scholar
  4. Berzofsky, J. A., 1983, T-B reciprocity. An Ia restricted epitopespecific circuit regulating T-cell - B-cell interaction and antibody specificity, Surv. Immunol. Res, 2:223.PubMedGoogle Scholar
  5. Bothwell, A. L. M., 1984, The genes encloding anti-NP antibodies in inbred strains of mice, in: The Biology of Idiotypes, Greene, M. I., and Nisonoff, A., Eds., Plenum Press, N. Y.Google Scholar
  6. Ceska, J. M., Stratton, J. A., Miller, A. and Sercarz, E., 1976, Structural aspects of immune recognition and its consequences for antibody specificity, Eur. J. Immunol., 6:639.CrossRefGoogle Scholar
  7. Crews, S., Griffin, J., Huang, H., Calame, K., and Hood, L., 1981, A single VH gene segment encodes the immune response to phosphorylcholine: somatic mutation is correlated with the class of antibody, Cell, 25:59.PubMedCrossRefGoogle Scholar
  8. Darsley, M. J., and Rees, A. R., 1985, Nucleotide sequences of fine antilysozyme monoclonal antibodies, EMBO J, 4:393.PubMedGoogle Scholar
  9. Fazakas de St. Groth, S, 1967, Cross recognition and cross reactivity. Cold Spring Harbor Symposium Quant. Biol., 32:525.Google Scholar
  10. Gray, D. I., MacLennan, C. M. and Lane, P. J., 1986, Virgin B cell recruitment and the life span of memory clones during antibody response to 2,4-dimitrophenyl hemocyanin, Eur. J. Immunol., 16:641.PubMedCrossRefGoogle Scholar
  11. Jerne, N. K. , 1974, Towards a network theory of the immune system, Ann. Immunol. (Paris), 125C:373.Google Scholar
  12. Kaartinen, M., Griffiths, G. M., Markham, A. F. and Milstein, C., 1983, MRNA sequences define an unusually restricted IgG response to 2phenyloxazolone and its early diversification, Nature, 304:320.PubMedCrossRefGoogle Scholar
  13. Kaiser, C. A. , Pruess, D., Grisafi, P. and Botslein, D., 1987, Many random sequences functionally replace the secretion signal sequence of yeast invertase, Science, 235:312.PubMedCrossRefGoogle Scholar
  14. Katz, M. E., Miller, A., Krzych, V., Wicker, L., Maizels, R., Clark, J., Shastri, N., Oki, A. and Sercarz, E., 1983, Hierarchial relationships among epitopes; only certain potentially utilizable epitopes on protein antigens are actually presented in a particular haplotype, in: In Gene: Past, Present, and Future. Pierce, C. W., Cohen, S. E., Kapp, J. A., Schwartz, B. D. and Schreffler, D. C., eds. Humana Press, Clifton N. J.Google Scholar
  15. Klinman, N. R. , 1972, The mechanism of antigenic stimulation of primary and secondary clonal precursor cells, J. Exp. Med., 136:241.PubMedCrossRefGoogle Scholar
  16. Klinman, N. R., Press, J. L. and Segal, G. P., 1973, Overlap stimulation of primary and secondary B cells by cross reacting determinants, J. Exp. Med., 138:1276.PubMedCrossRefGoogle Scholar
  17. Ma, J. and Ptashne, M., 1987, A new class of yeast transcriptional activators, Cell, 51:113.PubMedCrossRefGoogle Scholar
  18. Maizels, N. and Bothwell, A. , 1985, The T cell independent immune response to the hapten NP uses a large repertoire of heavy chain genes, Cell, 43:715.PubMedCrossRefGoogle Scholar
  19. Morrow, P. R., Renick, D. M. and Benjamini, E., 1983, The antibody response to a single antigenic determinant of the tobacco mosaic virus protein (TMVP) : Effect of allotype-linked genes and restricted heterogeneity of the response, J. Immunol., 131:2875.PubMedGoogle Scholar
  20. Mudgett-Hunter, M., Anderson, W., Haber, E. and Margolies, M. N., 1985, Bending and structural diversity among high affinity monoclonal antidigoxin antibodies, Mol. Immunol., 22:477.PubMedCrossRefGoogle Scholar
  21. Nahmias, C., Strassberg, A. D. and Emorine, L. J., 1988, The immune response towards β adrenergic ligands and their receptors, VIII, extensive diversity of VH and VL genes encoding anti-alprenolol antibodies, J. Immunol., 148:1304.Google Scholar
  22. Ogata, C., Hatada, M., Tomlinson, G., Shin, W. and Kim, S., 1987, Crystal structure of the intensely sweet protein monellin, Nature, 328:739.PubMedCrossRefGoogle Scholar
  23. Rennick, D. M., Morrow, P. R. and Benjamini, E., 1983, Immunological studies with tobacco mosaic virus protein: differential activation of B cell subpopulations, Adv. Exp. Med. and Biol., 150:201.CrossRefGoogle Scholar
  24. Riley, S. C., Connors, S. J., Klinman, N. K. and Ogata, R. T., 1986, Preferential expression of variable region heavy chain gene segments by predominant 2,4-dimitrophenyl-specific BALB/c neonatal antibody clonotype, Proc. Natl. Acad. Sci. (USA), 83:2589.CrossRefGoogle Scholar
  25. Schiff, C., Milili, M. and Fougereau, M., 1983, Immunoglobulin diversity: analysis of the germ live VH gene repertoire of the murine anti-GAT response, Nucleic Acid Res., 11:4007.PubMedCrossRefGoogle Scholar
  26. Slaohi, M., Leo, O., Marvel, J., Maser, M., Hierioux, J. and Urbain, J., 1984, Idiotypic analysis of potential and available repertoire in the arsonate system, J. Exp. Med., 160:1.CrossRefGoogle Scholar
  27. Wu, T. T. and Kabat, E. A., 1970, An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity, J. Exp. Med., 132:211.PubMedCrossRefGoogle Scholar
  28. Wysocki, L., Manser, T. and Gefter, M. L., 1986, Somatic evolution of variable region structures during an immune response, Proc. Natl. Acad. Sci. (USA), 83:1847.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Eli Benjamini
    • 1
  • Matthew L. Andria
    • 1
  • Soshana Levy
    • 2
  • Cherry Y. Leung
    • 1
  1. 1.Department of Medical Microbiology and Immunology, School of MedicineUniversity of CaliforniaDavisUSA
  2. 2.Department of Medicine, School of MedicineStanford UniversityStanfordUSA

Personalised recommendations