Skip to main content
PMC home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1973 Feb 28;137(3):636–648. doi: 10.1084/jem.137.3.636

AN IDIOTYPIC CROSS-REACTION BETWEEN ALLOTYPE a3 AND ALLOTYPE a NEGATIVE RABBIT ANTIBODIES TO STREPTOCOCCAL CARBOHYDRATE

Thomas J Kindt 1, David G Klapper 1, Michael D Waterfield 1
PMCID: PMC2139383  PMID: 4120286

Abstract

Two antibodies to Group C streptococcal carbohydrate isolated from an individual rabbit had similar relative binding affinities for a Group C immuno-adsorbent column. Their light chains were similar, if not identical, as were the constant regions of their heavy chains. Differences in the variable regions of the H chains of the two antibodies were detected by chemical analysis. The two antibodies had serologically identical idiotypic determinants although one antibody possessed the a3 allotype and the other had no detectable group a marker. The occurrence of such antibodies indicates the absence of obligatory associations between group a allotypes and idiotypic specificities, despite the fact that both determinants have antigenic components in the VH region of the H chain.

Full Text

The Full Text of this article is available as a PDF (872.0 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blomberg B., Geckeler W. R., Weigert M. Genetics of the antibody response to dextran in mice. Science. 1972 Jul 14;177(4044):178–180. doi: 10.1126/science.177.4044.178. [DOI] [PubMed] [Google Scholar]
  2. Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem. 1970 Jun;245(12):3059–3065. [PubMed] [Google Scholar]
  3. Eichmann K., Greenblatt J. Relationships between relative binding affinity and electrophoretic behavior of rabbit antibodies to streptococcal carbohydrates. J Exp Med. 1971 Mar 1;133(3):424–441. doi: 10.1084/jem.133.3.424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Eichmann K., Kindt T. J. The inheritance of individual antigenic specificities of rabbit antibodies to streptococcal carbohydrates. J Exp Med. 1971 Aug 1;134(2):532–552. doi: 10.1084/jem.134.2.532. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. FLEISCHMAN J. B., PORTER R. R., PRESS E. M. THE ARRANGEMENT OF THE PEPTIDE CHAINS IN GAMMA-GLOBULIN. Biochem J. 1963 Aug;88:220–228. doi: 10.1042/bj0880220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gally J. A., Edelman G. M. Somatic translocation of antibody genes. Nature. 1970 Jul 25;227(5256):341–348. doi: 10.1038/227341a0. [DOI] [PubMed] [Google Scholar]
  7. HEYMANN H., MANNIELLO J. M., ZELEZNICK L. D., BARKULIS S. S. STRUCTURE OF STREPTOCOCCAL CELL WALLS. II. GROUP A BIOSE AND GROUP A TRIOSE FROM C-POLYSACCHARIDE. J Biol Chem. 1964 May;239:1656–1663. [PubMed] [Google Scholar]
  8. Habeeb A. F. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal Biochem. 1966 Mar;14(3):328–336. doi: 10.1016/0003-2697(66)90275-2. [DOI] [PubMed] [Google Scholar]
  9. Kindt T. J., Seide R. K., Lackland H., Thunberg A. L. Serologic identity of the b4 allotypic determinants present on homogeneous rabbit light chains with different N-terminal amino acid sequences. J Immunol. 1972 Oct;109(4):735–741. [PubMed] [Google Scholar]
  10. Kindt T. J., Todd C. W., Eichmann K., Krause R. M. Allotype exclusion in uniform rabbit antibody to streptococcal carbohydrate. J Exp Med. 1970 Feb;131(2):343–354. doi: 10.1084/jem.131.2.343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Krause R. M. The search for antibodies with molecular uniformity. Adv Immunol. 1970;12:1–56. doi: 10.1016/s0065-2776(08)60167-4. [DOI] [PubMed] [Google Scholar]
  12. Kuettner M. G., Wang A. L., Nisonoff A. Quantitative investigations of idiotypic antibodies. VI. Idiotypic specificity as a potential genetic marker for the variable regions of mouse immunoglobulin polypeptide chains. J Exp Med. 1972 Mar 1;135(3):579–595. doi: 10.1084/jem.135.3.579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kunkel H. G., Agnello V., Joslin F. G., Winchester R. J., Capra J. D. Cross-idiotypic specificity among monoclonal IgM proteins with anti- -globulin activity. J Exp Med. 1973 Feb 1;137(2):331–342. doi: 10.1084/jem.137.2.331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mole L. E., Jackson S. A., Porter R. R., Wilkinson J. M. Allotypically related sequences in the Fd fragment of rabbit immunoglobulin heavy chains. Biochem J. 1971 Sep;124(2):301–318. doi: 10.1042/bj1240301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Oudin J., Michel M. Idiotypy of rabbit antibodies. II. Comparison of idiotypy of various kinds of antibodies formed in the same rabbits against Salmonella typhi. J Exp Med. 1969 Sep 1;130(3):619–642. doi: 10.1084/jem.130.3.619. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Penn G. M., Kunkel H. G., Grey H. M. Sharing of individual antigenic determinants between a gamma G and a gamma M protein in the same myeloma serum. Proc Soc Exp Biol Med. 1970 Dec;135(3):660–665. doi: 10.3181/00379727-135-35116. [DOI] [PubMed] [Google Scholar]
  17. TODD C. W. Allotypy in rabbit 19S protein. Biochem Biophys Res Commun. 1963 May 3;11:170–175. doi: 10.1016/0006-291x(63)90329-2. [DOI] [PubMed] [Google Scholar]
  18. Tosi S. L., Mage R. G., Gilman-Sachs A., Dray S., Knight K. L. Presence of the Fc-fragment allotypic determinant, A15, on IgG from an allotype-suppressed Aa2 homozygous rabbit lacking the Aa2 determinants of the Fd fragment. J Immunol. 1972 Jan;108(1):264–267. [PubMed] [Google Scholar]
  19. Waterfield M. D., Prahl J. W., Hood L. E., Kindt T. J., Krause R. M. Restricted structural heterogeneity in antibodies: might different heavy chains have a common light chain? Nat New Biol. 1972 Dec 13;240(102):215–217. doi: 10.1038/newbio240215a0. [DOI] [PubMed] [Google Scholar]
  20. Wilkinson J. M. Variation in the N-terminal sequence of heavy chains of immunoglobulin G from rabbits of different allotype. Biochem J. 1969 Apr;112(2):173–185. doi: 10.1042/bj1120173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Willims R. C., Jr, Kunkel H. G., Capra J. D. Antigenic specificities related to the cold agglutinin activity of gamma M globulins. Science. 1968 Jul 26;161(3839):379–381. doi: 10.1126/science.161.3839.379. [DOI] [PubMed] [Google Scholar]
  22. Wilson S. K., Brient B. W., Nisonoff A. Individually specific antigenic determinants shared by a myeloma protein and nonspecific IgG. Ann N Y Acad Sci. 1971 Dec 31;190:362–370. doi: 10.1111/j.1749-6632.1971.tb13548.x. [DOI] [PubMed] [Google Scholar]
  23. Wu T. T., Kabat E. A. 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. 1970 Aug 1;132(2):211–250. doi: 10.1084/jem.132.2.211. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES