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. 1982 Jul;79(14):4391–4394. doi: 10.1073/pnas.79.14.4391

BASILEA rabbits express two types of immunoglobulin light chains: lambda and kappa-like.

I Garcia, D C Brandt, A Benammar, P A Cazenave, J C Jaton
PMCID: PMC346677  PMID: 6812047

Abstract

In the variant rabbit strain BASILEA, immunoglobulin G were shown to contain two distinct populations of IgG molecules whose light (L) chains belonged to the known lambda isotype and to a new kappa-like type. These two L chains differed from each other by electrophoretic, chemical, and antigenic properties. The kappa-like L chain fraction showed (i) an acid-labile Asp-Pro bond at the end of the joining region and (ii) a tryptic peptide, whose amino acid sequence of the NH2-terminal 15 residues was identical to the homologous constant (C) region sequence of b9 kappa chain with the exception of the residue in position 70, which is asparagine in the kappa-like chain instead of the characteristic half-cystine residue in all L chains of kappa B type expressing b4, b5, b6, or b9 allotypes. The data suggest that the kappa-like L chain component does not contain the C region half-cystine residue involved in the formation of the extra variable (V) region-C region disulfide bridge in L chains of the kappa B [Rejnek, J., Appella, E., Mage, R. G. & Reisfeld, R. A. (1969) Biochemistry 8, 2712-2718]. The partial NH2-terminal amino acid sequence of the C region of the kappa-like L chain was shown to be markedly different from b4, b6, or b9 region sequences and from rabbit lambda C region sequence. Taken together, the chemical data suggest that the kappa bas component represents a new subtype of kappa chain. A rabbit alloantiserum made against bas IgG and adsorbed with IgG fractions showing b4, b5, b6, b95, and b96 L chain allotypes appeared to be directed against the kappa-like L chain component of BASILEA IgG exclusively. All BASILEA animals expressed IgG molecules containing kappa-like chains; in contrast, IgG molecules derived from the standard domestic rabbit did not react with this antiserum.

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Selected References

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

  1. Appella E., Chersi A., Rejnek J., Reisfeld R., Mage R. Rabbit immunoglobulin lambda chains: isolation and amino acid sequence of cysteine-containing peptides. Immunochemistry. 1974 Aug;11(8):395–402. doi: 10.1016/0019-2791(74)90072-x. [DOI] [PubMed] [Google Scholar]
  2. Appella E., Roholt O. A., Chersi A., Radzimski G., Pressman D. Amino acid sequence of the light chain derived from a rabbit anti-p-azobenzoate antibody of restricted heterogeneity. Biochem Biophys Res Commun. 1973 Aug 21;53(4):1122–1129. doi: 10.1016/0006-291x(73)90581-0. [DOI] [PubMed] [Google Scholar]
  3. Avrameas S., Ternynck T. The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents. Immunochemistry. 1969 Jan;6(1):53–66. doi: 10.1016/0019-2791(69)90178-5. [DOI] [PubMed] [Google Scholar]
  4. Brandt D. C., Jaton J. C. Occurrence of idiotypically identical antibodies in the sera of two outbred rabbits hyperimmunized with type II pneumococcal vaccine. J Immunol. 1978 Sep;121(3):1188–1193. [PubMed] [Google Scholar]
  5. Brezin C., Cazenave P. A. La réaction croisee entre le motif allotypique Aa1 des immunoglobulines du lapin et les anticorps dirigés contre le motif allotypique Aa3: participation des variantes de la spécificité Aa1 à cette réaction croiśee. Immunochemistry. 1975 Mar;12(3):241–247. doi: 10.1016/0019-2791(75)90238-4. [DOI] [PubMed] [Google Scholar]
  6. Cambiaso C. L., Goffinet A., Vaerman J. P., Heremans J. F. Glutaraldehyde-activated aminohexyl- derivative of Sepharose 4B as a new verstile immunoabsorbent. Immunochemistry. 1975 Apr;12(4):273–278. doi: 10.1016/0019-2791(75)90175-5. [DOI] [PubMed] [Google Scholar]
  7. Chen K. C., Kindt T. J., Krause R. M. Primary structure of the L chain from a rabbit homogeneous antibody to streptococcal carbohydrate. II. Sequence determination of peptides from tryptic and peptic digests. J Biol Chem. 1975 May 10;250(9):3289–3296. [PubMed] [Google Scholar]
  8. Dubiski S., Muller P. J. A "new" allotypic specificity (A9) of rabbit immunoglobulin. Nature. 1967 May 13;214(5089):696–697. doi: 10.1038/214696a0. [DOI] [PubMed] [Google Scholar]
  9. Emorine L., Dutka S., Paroutaud P., Strosberg A. D. The structural correlates of the rabbit light chain b allotypes: sequence studies of b5 and b6 chains. Mol Immunol. 1979 Dec;16(12):997–1004. doi: 10.1016/0161-5890(79)90033-6. [DOI] [PubMed] [Google Scholar]
  10. Farnsworth V., Goodfliesh R., Rodkey S., Hood L. Immunoglobulin allotypes of rabbit kappa chains: polymorphism of a control mechanism regulating closely linked duplicated genes? Proc Natl Acad Sci U S A. 1976 Apr;73(4):1293–1296. doi: 10.1073/pnas.73.4.1293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fraser K. J., Pulsen K., Haber E. Specific cleavage between variable and constant domains of rabbit antibody light chains by dilute acid hydrolysis. Biochemistry. 1972 Dec 19;11(26):4974–4977. doi: 10.1021/bi00776a016. [DOI] [PubMed] [Google Scholar]
  12. GREENWOOD F. C., HUNTER W. M., GLOVER J. S. THE PREPARATION OF I-131-LABELLED HUMAN GROWTH HORMONE OF HIGH SPECIFIC RADIOACTIVITY. Biochem J. 1963 Oct;89:114–123. doi: 10.1042/bj0890114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Garcia I., Jaton J. C. The immune response to type II and type VIII pneumococcal vaccines in Basilea rabbits lacking K light chains. Immunochemical and partial amino acid sequence studies of the light chains. Mol Immunol. 1979 Dec;16(12):1063–1071. doi: 10.1016/0161-5890(79)90040-3. [DOI] [PubMed] [Google Scholar]
  14. Garcia I., Jaton J. C. The primary structure of the constant region of Basilea-rabbit immunoglobulin lambda-chains. Biochem J. 1981 Jul 1;197(1):177–183. doi: 10.1042/bj1970177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Good P. W., Notenboom R., Dubiski S., Cinader B. Basilea rabbit immunoglobulins: detection and characterization by specific alloantiserum. J Immunol. 1980 Sep;125(3):1293–1297. [PubMed] [Google Scholar]
  16. Hieter P. A., Korsmeyer S. J., Waldmann T. A., Leder P. Human immunoglobulin kappa light-chain genes are deleted or rearranged in lambda-producing B cells. Nature. 1981 Apr 2;290(5805):368–372. doi: 10.1038/290368a0. [DOI] [PubMed] [Google Scholar]
  17. Jaton J. C. Amino acid sequence of the N-terminal 139 residues of light chain derived from a homogeneous rabbit antibody. Biochem J. 1974 Jul;141(1):1–13. doi: 10.1042/bj1410001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Kelus A. S., Weiss S. Variant strain of rabbits lacking immunoglobulin kappa polypeptide chain. Nature. 1977 Jan 13;265(5590):156–158. doi: 10.1038/265156a0. [DOI] [PubMed] [Google Scholar]
  19. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  20. O'Donnell I. J., Frangione B., Porter R. R. The disulphide bonds of the heavy chain of rabbit immunoglobulin G. Biochem J. 1970 Jan;116(2):261–268. doi: 10.1042/bj1160261. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. OUDIN J. Allotypy of rabbit serum proteins. I. Immuno-chemical analysis leading to the individualization of seven main allotypes. J Exp Med. 1960 Jul 1;112:107–124. doi: 10.1084/jem.112.1.107. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. OUDIN J. Allotypy of rabbit serum proteins. II. Relationships between various allotypes: their common antigenic specificity, their distribution in a sample population; genetic implications. J Exp Med. 1960 Jul 1;112:125–142. doi: 10.1084/jem.112.1.125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. OUDIN J. L'allotypie de certains antigènes protéidiques du sérum. C R Hebd Seances Acad Sci. 1956 May 23;242(21):2606–2608. [PubMed] [Google Scholar]
  24. Rejnek J., Appella E., Mage R. G., Reisfeld R. A. Subtypes of rabbit kappa light polypeptide chains associated with the beta locus. Biochemistry. 1969 Jul;8(7):2712–2718. doi: 10.1021/bi00835a004. [DOI] [PubMed] [Google Scholar]
  25. Sogn J. A., Kindt T. J. A genetic polymorphism in the constant region of rabbit b4 kappa chains. J Exp Med. 1976 Jun 1;143(6):1475–1482. doi: 10.1084/jem.143.6.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Strosberg A. D., Hamers-Casterman C., Van der Loo W., Hamers R. A rabbit with the allotypic phenotype: ala2a3 b4b5b6. J Immunol. 1974 Oct;113(4):1313–1318. [PubMed] [Google Scholar]
  27. Tarr G. E., Beecher J. F., Bell M., McKean D. J. Polyquarternary amines prevent peptide loss from sequenators. Anal Biochem. 1978 Feb;84(2):622–7?0=ENG. doi: 10.1016/0003-2697(78)90086-6. [DOI] [PubMed] [Google Scholar]
  28. Weiss S., Hild K., Braun D. G. Light chain heterogeneity of type lambda anti-streptococcal group A-variant polysaccharide antibodies in rabbits. Immunobiology. 1979 Aug;156(1-2):35–40. [PubMed] [Google Scholar]
  29. Weiss S., Kelus A. S., Braun D. G. Antibody response to the streptococcal group A-variant polysaccharide in BASILEA rabbits lacking kappa-polypeptide chains. J Exp Med. 1977 Nov 1;146(5):1195–1205. doi: 10.1084/jem.146.5.1195. [DOI] [PMC free article] [PubMed] [Google Scholar]

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