Skip to main content
NCBI home page
Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1977 Nov;30(2):233–241.

An immunoglobulin heavy chain variable region (VH) marker associated with cross-reactive idiotypes in man.

T Feizi, J Lecomte, R Childs
PMCID: PMC1541133  PMID: 414866

Abstract

The VH specificities of two rabbit antisera raised against the H chains of two human IgM cold agglutinins were studied with the aid of proteins on which the VH sequence data are available. They were found to recognize a new VH antigen (VHMar), which may represent a subgroup of VHI. This antigen is found on anti-Ii antibodies which have cross-reactive idiotypes. It is moderately well-expressed in normal gamma globulin and strongly expressed on 8% of unselected myeloma and macroglobulinaemia proteins. There is evidence to suggest that a proportion of the cross-reactive idiotypes among the anti-Ii antibodies involve this VH antigen.

Full text

PDF
233

Selected References

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

  1. BOYDEN S. V. The adsorption of proteins on erythrocytes treated with tannic acid and subsequent hemagglutination by antiprotein sera. J Exp Med. 1951 Feb;93(2):107–120. doi: 10.1084/jem.93.2.107. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Capra J. D., Kehoe J. M. Distribution and association of heavy and light chain variable region subgroups among human IgA immunoglobulins. J Immunol. 1975 Feb;114(2 Pt 1):678–681. [PubMed] [Google Scholar]
  3. Capra J. D., Kehoe J. M. Variable region sequences of five human immunoglobulin heavy chains of the VH3 subgroup: definitive identification of four heavy chain hypervariable regions. Proc Natl Acad Sci U S A. 1974 Mar;71(3):845–848. doi: 10.1073/pnas.71.3.845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Childs R., Feizi T. Cross idiotypic specificity among heavy chains of macroglobulins with blood group I and i specificities. Nature. 1975 Jun 12;255(5509):562–564. doi: 10.1038/255562a0. [DOI] [PubMed] [Google Scholar]
  5. Cooper A. G., Chavin S. I., Franklin E. C. Predominance of a single mu chain subclass in cold agglutinin heavy chains. Immunochemistry. 1970 May;7(5):479–483. doi: 10.1016/0019-2791(70)90230-2. [DOI] [PubMed] [Google Scholar]
  6. Cunningham B. A., Pflumm M. N., Rutishauser U., Edelman G. M. Subgroups of amino acid sequences in the variable regions of immunoglobulin heavy chains. Proc Natl Acad Sci U S A. 1969 Nov;64(3):997–1003. doi: 10.1073/pnas.64.3.997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Edelman G. M., Cunningham B. A., Gall W. E., Gottlieb P. D., Rutishauser U., Waxdal M. J. The covalent structure of an entire gammaG immunoglobulin molecule. Proc Natl Acad Sci U S A. 1969 May;63(1):78–85. doi: 10.1073/pnas.63.1.78. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Feizi T., Kunkel H. G., Roelcke D. Cross idiotypic specificity among cold agglutinins in relation to combining activity for blood group-related antigens. Clin Exp Immunol. 1974 Oct;18(2):283–293. [PMC free article] [PubMed] [Google Scholar]
  9. Feizi T., Lecomte J., Childs R., Solomon A. Kappa chain (V kappa III) subgroup-related activity in an idiotypic anti-cold agglutinin serum. Scand J Immunol. 1976;5(6-7):629–636. doi: 10.1111/j.1365-3083.1976.tb03012.x. [DOI] [PubMed] [Google Scholar]
  10. Fisher C. E., Palm W. H., Press E. M. The N-terminal sequence of a human gamma 1 chain of allotype Gm(a(-)f(+)). FEBS Lett. 1969 Sep;5(1):20–22. doi: 10.1016/0014-5793(69)80282-6. [DOI] [PubMed] [Google Scholar]
  11. Florent G., Lehman D., Putnam F. W. The switch point in mu heavy chains of human IgM immunoglobulins. Biochemistry. 1974 Jun 4;13(12):2482–2498. doi: 10.1021/bi00709a004. [DOI] [PubMed] [Google Scholar]
  12. Franklin E. C., Frangione B. Common structural and antigenic properties of human gamma M anti-gamma globulins. J Immunol. 1971 Dec;107(6):1527–1534. [PubMed] [Google Scholar]
  13. Franklin E. C., Frangione B. Structural differences between macroglobulins belonging to two serologically distinguishable subclasses. Biochemistry. 1968 Dec;7(12):4203–4211. doi: 10.1021/bi00852a010. [DOI] [PubMed] [Google Scholar]
  14. Franklin E. C., Frangione B. Two serologically distinguishable subclasses of mu-chains of human macroglobulins. J Immunol. 1967 Oct;99(4):810–814. [PubMed] [Google Scholar]
  15. Gergely J., Wang A. C., Fudenberg H. H. Chemical analyses of variable regions of heavy and light chains of cold agglutinins. Vox Sang. 1973 May;24(5):432–440. doi: 10.1111/j.1423-0410.1973.tb03484.x. [DOI] [PubMed] [Google Scholar]
  16. Kaplan A. P., Hood L. E., Terry W. D., Metzger H. Amino terminal sequences of human immunoglobulin heavy chains. Immunochemistry. 1971 Sep;8(9):801–811. doi: 10.1016/0019-2791(71)90447-2. [DOI] [PubMed] [Google Scholar]
  17. Kratzin H., Altevogt P., Ruban E., Kortt A., Staroscik K., Hilschmann N. Die Primärstruktur eines monoklonalen IgA-Immunoglobulins (IgA Tro.), II. Die Aminosäuresequenz der H-Kette, alpha-Typ, Subgruppe III. Struktur des gesamten IgA-Moleküls. Hoppe Seylers Z Physiol Chem. 1975 Aug;356(8):1337–1342. [PubMed] [Google Scholar]
  18. Kunkel H. G., Winchester R. J., Joslin F. G., Capra J. D. Similarities in the light chains of anti-gamma-globulins showing cross-idiotypic specificities. J Exp Med. 1974 Jan 1;139(1):128–136. doi: 10.1084/jem.139.1.128. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Laure C. J., Watanabe S., Hilschmann N. Die Primärstruktur eines monoklonalen IgM-Immunoglobulins (Makroglobulin Gal.),I. Die Aminosäuresequenz der L-Kette, kappa-Typ, Subgruppe I. Hoppe Seylers Z Physiol Chem. 1973 Oct-Nov;354(10-11):1503–1504. [PubMed] [Google Scholar]
  20. Lecomte J., Feizi T. A common idiotype on human macroglobulins with anti-I and anti-i specificity. Clin Exp Immunol. 1975 May;20(2):287–302. [PMC free article] [PubMed] [Google Scholar]
  21. Oudin J., Cazenave P. A. Similar idiotypic specificities in immunoglobulin fractions with different antibody functions or even without detectable antibody function. Proc Natl Acad Sci U S A. 1971 Oct;68(10):2616–2620. doi: 10.1073/pnas.68.10.2616. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pitcher S. E., Konigsberg W. The sequence of the NH2-terminal cyanogen bromide fragment from the heavy chain of a gamma-G1 myeloma protein. J Biol Chem. 1970 Mar 25;245(6):1267–1274. [PubMed] [Google Scholar]
  23. Putnam F. W., Florent G., Paul C., Shinoda T., Shimizu A. Complete amino acid sequence of the Mu heavy chain of a human IgM immunoglobulin. Science. 1973 Oct 19;182(4109):287–291. doi: 10.1126/science.182.4109.287. [DOI] [PubMed] [Google Scholar]
  24. Solomon A., McLaughlin C. L. Bence Jones proteins and light chains of immunoglobulins. IV. Immunochemical differentiation among proteins within each of the three established kappa-chain classes. J Immunol. 1971 Jan;106(1):120–127. [PubMed] [Google Scholar]
  25. 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]
  26. Wolfenstein-Todel C., Frangione B., Franklin E. C. Partial amino acid sequence of an IgA2 human immunoglobulin heavy chain. Biochim Biophys Acta. 1975 Feb 27;379(2):627–637. doi: 10.1016/0005-2795(75)90169-5. [DOI] [PubMed] [Google Scholar]
  27. Wolfenstein-Todel C., Franklin E. C., Rudders R. A. Similarities of the light chains and the variable regions of the heavy chains of the IgG2 lambda and IgA1 lambda myeloma proteins from a single patient. J Immunol. 1974 Mar;112(3):871–876. [PubMed] [Google Scholar]

Articles from Clinical and Experimental Immunology are provided here courtesy of British Society for Immunology

RESOURCES