Skip to main content
PMC home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1974 Jan 1;139(1):159–179. doi: 10.1084/jem.139.1.159

IMMUNOCHEMICAL STUDIES ON MOUSE MYELOMA PROTEINS REACTIVE WITH DEXTRANS OR WITH FRUCTOSANS AND ON HUMAN ANTILEVANS

John Cisar 1, Elvin A Kabat 1, Jerry Liao 1, Michael Potter 1
PMCID: PMC2139512  PMID: 4808707

Abstract

Four BALB/c IgA mouse myeloma proteins (W3129, W3434, QUPC 52, and UPC 102) reactive with dextran, four myeloma proteins reactive with fructosans, three IgA (W3082, UPC 61, and Y5476), and one IgG2a (UPC 10), and two human antilevans were studied immunochemically. Quantitative precipitin and inhibition assays showed that W3129, W3434, and QUPC 52 had specificities for isomaltose oligosaccharides similar to those previously found with α(1 → 6)-specific human antidextrans. W3129 and W3434 were most complementary to IM5 but W3129 reacted equally with IM4 and IM3 while W3434 had a greater affinity for IM4 than IM3. QUPC 52 had a larger combining region and was most complementary to IM6. Protein UPC 102 (IgA), like MOPC 104E (IgM) (27), was most complementary to the α(1 → 3)-linked trisaccharide, nigerotriose, and thus differed from J558 (29), which was inhibited best by nigeropentaose. UPC 102 was similar to J558 but they differed from MOPC 104E in their reactions with non-α(1 → 3)-linked disaccharides. The fructosan-specific myeloma proteins fell into two groups with different specificities. The first group, W3082 (IgA), UPC 61 (IgA), and the previously studied J606 (IgG3) (28, 29), reacted with inulin and W3082 and UPC 61 appeared to have identical specificities for β(2 → 1)-linked fructofuranosyl residues with maximum complementarity for the tetrasaccharide βDfructofuranosyl (2 → 1)βDfructofuranosyl(2 → 1)βDfructofuranosyl(2 → 6)Dglucose while protein J606 was inhibited best by the trisaccharide βDfructofuranosyl(2 → 1)βDfructofuranosyl(2 → 6)Dglucose. W3082 and UPC 61 also differed from J606 in their behavior toward sucrose and βDfructofuranosyl(2 → 6)Dglucose as compared with αDglucosyl(1 → 3)Dfructose (turanose). The second group containing myeloma proteins UPC 10 (IgG2a) and Y5476 (IgA) behaved similarly to human antilevans in that neither reacted with inulin nor were they inhibited by the β(2 → 1)-linked fructose oligosaccharides. Unlike the β(2 → 1)-specific proteins, they reacted with perennial rye grass levan that contained over 90% β(2 → 6)links. The differences in specificity and site size among homogeneous mouse myeloma proteins reactive with the same antigenic determinant are completely consistent with the concept that they represent products of homogeneous clones selected from the known heterogeneous population of antibody-forming cells.

Full Text

The Full Text of this article is available as a PDF (1.1 MB).

Selected References

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

  1. ALLEN P. Z., KABAT E. A. Studies on the capacity of some polysaccharides to elicit antibody formation in man. J Exp Med. 1957 May 1;105(5):383–394. doi: 10.1084/jem.105.5.383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ballou C. E. A study of the immunochemistry of three yeast mannans. J Biol Chem. 1970 Mar 10;245(5):1197–1203. [PubMed] [Google Scholar]
  3. Eisen H. N., Simms E. S., Potter M. Mouse myeloma proteins with antihapten antibody acitivity. The protein produced by plasma cell tumor MOPC-315. Biochemistry. 1968 Nov;7(11):4126–4134. doi: 10.1021/bi00851a048. [DOI] [PubMed] [Google Scholar]
  4. GELZER J., KABAT E. A. SPECIFIC FRACTIONATION OF HUMAN ANTI-DEXTRAN ANTIBODIES. 3. FRACTIONATION OF ANTI-DEXTRAN BY SEQUENTIAL EXTRACTION WITH OLIGOSACCHRIDES OF INCREASING CHAIN LENGTH AND ATTEMPTS AT SUBFRACTIONATION. Immunochemistry. 1964 Dec;1:303–316. [PubMed] [Google Scholar]
  5. GELZER J., KABAT E. A. SPECIFIC FRACTIONATION OF HUMAN ANTIDEXTRAN ANTIBODIES. II. ASSAY OF HUMAN ANTIDEXTRAN SERA AND SPECIFICALLY FRACTIONATED PURIFIED ANTIBODIES BY MICROCOMPLEMENT FIXATION AND COMPLEMENT FIXATION INHIBITION TECHNIQUES. J Exp Med. 1964 Jan 1;119:983–995. doi: 10.1084/jem.119.6.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. GOODMAN J. W., KABAT E. A. Immunochemical studies on cross-reactions of antipneumococcal sera. I. Cross-reactions of types II and XX antipneumococcal sera with dextrans and of type II antipneumococcal serum with glycogen and Friedlaender type B polysaccharide. J Immunol. 1960 Apr;84:333–346. [PubMed] [Google Scholar]
  7. GOODMAN J. W., KABAT E. A. Immunochemical studies on cross-reactions of antipneumococcal sera. II. Cross-reactions of types IX and XII antipneumococcal sera with dextrans. J Immunol. 1960 Apr;84:347–357. [PubMed] [Google Scholar]
  8. Grey H. M., Hirst J. W., Cohn M. A new mouse immunoglobulin: IgG3. J Exp Med. 1971 Feb 1;133(2):289–304. doi: 10.1084/jem.133.2.289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Harisdangkul V., Kabat E. A. Studies on human antibodies. IX. Interaction of 1-(m-nitrophenyl)-flavazoles of isomaltose oligosaccharides with purified antidextrans: quantitative hapten-inhibition and fluorescence quenching studies. J Immunol. 1972 May;108(5):1232–1243. [PubMed] [Google Scholar]
  10. Hehre E. J., Neill J. M. FORMATION OF SEROLOGICALLY REACTIVE DEXTRANS BY STREPTOCOCCI FROM SUBACUTE BACTERIAL ENDOCARDITIS. J Exp Med. 1946 Jan 31;83(2):147–162. [PMC free article] [PubMed] [Google Scholar]
  11. Jaffe B. M., Eisen H. N., Simms E. S., Potter M. Myeloma proteins with anti-hapten antibody activity: epsilon-2,4-dinitrophenyl lysine binding by the protein produced by mouse plasmacytoma MOPC-460. J Immunol. 1969 Oct;103(4):872–874. [PubMed] [Google Scholar]
  12. Johnston I. R. The partial acid hydrolysis of a highly dextrorotatory fragment of the cell wall of Aspergillus niger. Isolation of the alpha-(1-3)-linked dextrin series. Biochem J. 1965 Sep;96(3):659–664. doi: 10.1042/bj0960659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. KABAT E. A., BERG D. Dextran; an antigen in man. J Immunol. 1953 Jun;70(6):514–532. [PubMed] [Google Scholar]
  14. KABAT E. A. Heterogeneity in extent of the combining regions of human antidextran. J Immunol. 1956 Dec;77(6):377–385. [PubMed] [Google Scholar]
  15. KABAT E. A. Immunochemical contributions to the elucidation of dextran structure. Bull Soc Chim Biol (Paris) 1960;42:1549–1568. [PubMed] [Google Scholar]
  16. KABAT E. A. Size and heterogeneity of the combining sites on an antibody molecule. J Cell Physiol Suppl. 1957 Dec;50(Suppl 1):79–102. doi: 10.1002/jcp.1030500406. [DOI] [PubMed] [Google Scholar]
  17. KABAT E. A. The upper limit for the size of the human antidextran combining site. J Immunol. 1960 Jan;84:82–85. [PubMed] [Google Scholar]
  18. Leon M. A., Young N. M., McIntire K. R. Immunochemical studies of the reaction between a mouse myeloma macroglobulin and dextrans. Biochemistry. 1970 Feb 17;9(4):1023–1030. doi: 10.1021/bi00806a043. [DOI] [PubMed] [Google Scholar]
  19. Lundblad A., Steller R., Kabat E. A., Hirst J. W., Weigert M. G., Cohn M. Immunochemical studies on mouse myeloma proteins with specificity for dextran or for levan. Immunochemistry. 1972 May;9(5):535–544. doi: 10.1016/0019-2791(72)90063-8. [DOI] [PubMed] [Google Scholar]
  20. MAGE R. G., KABAT E. A. IMMUNOCHEMICAL STUDIES ON DEXTRANS. III. THE SPECIFICITIES OF RABBIT ANTIDEXTRANS. FURTHER FINDINGS ON ANTIDEXTRANS WITH 1,2- AND 1,6-SPECIFICITIES. J Immunol. 1963 Nov;91:633–640. [PubMed] [Google Scholar]
  21. Moreno C., Kabat E. A. Studies on human antibodies. 8. Properties and association constants of human antibodies to blood group A substance purified with insoluble specific adsorbents and fractionally fluted with mono- and oligosaccharide. J Exp Med. 1969 May 1;129(5):871–896. doi: 10.1084/jem.129.5.871. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. POTTER M., BOYCE C. R. Induction of plasma-cell neoplasms in strain BALB/c mice with mineral oil and mineral oil adjuvants. Nature. 1962 Mar 17;193:1086–1087. doi: 10.1038/1931086a0. [DOI] [PubMed] [Google Scholar]
  23. Potter M. Immunoglobulin-producing tumors and myeloma proteins of mice. Physiol Rev. 1972 Jul;52(3):631–719. doi: 10.1152/physrev.1972.52.3.631. [DOI] [PubMed] [Google Scholar]
  24. Potter M., Leon M. A. Three IgA myeloma immunoglobulins from the BALB/ mouse: precipitation with pneumococcal C polysaccharide. Science. 1968 Oct 18;162(3851):369–371. doi: 10.1126/science.162.3851.369. [DOI] [PubMed] [Google Scholar]
  25. Potter M., Mushinski E. B., Glaudemans C. P. Antigen-binding IgA myeloma proteins in mice: specificities to antigens containing -D 1 leads to 6 linked galactose side chains and a protein antigen in wheat. J Immunol. 1972 Feb;108(2):295–300. [PubMed] [Google Scholar]
  26. Rovis L., Kabat E. A., Potter M. Immunochemical studies on a mouse myeloma protein having specific binding affinity for 2-acetamido-2-deoxy-D-mannose. Carbohydr Res. 1972 Jul;23(2):223–227. doi: 10.1016/s0008-6215(00)88028-3. [DOI] [PubMed] [Google Scholar]
  27. SCHIFFMAN G., KABAT E. A., THOMPSON W. IMMUNOCHEMICAL STUDIES ON BLOOD GROUPS. XXX. CLEAVAGE OF A, B, AND H BLOOD-GROUP SUBSTANCES BY ALKALI. Biochemistry. 1964 Jan;3:113–120. doi: 10.1021/bi00889a018. [DOI] [PubMed] [Google Scholar]
  28. SCHLOSSMAN S. F., KABAT E. A. Specific fractionation of a population of antidextran molecules with combining sites of various sizes. J Exp Med. 1962 Oct 1;116:535–552. doi: 10.1084/jem.116.4.535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Sher A., Tarikas H. Hapten binding studies on mouse IgA myeloma proteins with antibody activity. J Immunol. 1971 May;106(5):1227–1233. [PubMed] [Google Scholar]
  30. Suzuki S., Sunayama H., Saito T. Studies on the antigenic activity of yeasts. I. Analysis of the determinant groups of the mannan of Saccharomyces cerevisiae. Jpn J Microbiol. 1968 Mar;12(1):19–24. doi: 10.1111/j.1348-0421.1968.tb00365.x. [DOI] [PubMed] [Google Scholar]
  31. Suzuki S., Sunayama H. Studies on the antigenic activities of yeasts. II. Isolation and inhibition assay of the oligosaccharides from acetolysate of the mannan of Candida albicans. Jpn J Microbiol. 1968 Dec;12(4):413–422. doi: 10.1111/j.1348-0421.1968.tb00414.x. [DOI] [PubMed] [Google Scholar]
  32. Tarentino A. L., Maley F. The enzymic synthesis of O-alpha-D-glucopyranosyl (1-6)-2-amino-2-deoxy-D-glucopyranose and its N-acetyl derivative. Arch Biochem Biophys. 1969 Mar;130(1):80–85. doi: 10.1016/0003-9861(69)90012-5. [DOI] [PubMed] [Google Scholar]
  33. Torii M., Kabat E. A., Weigel H. Immunochemical studies on dextrans. IV. Further characterization of the determinant groups on various dextrans involved in their reactions with the homologous human antidextrans. J Immunol. 1966 May;96(5):797–805. [PubMed] [Google Scholar]
  34. Vicari G., Sher A., Cohn M., Kabat E. A. Immunochemical studies on a mouse myeloma protein with specificity for certain beta-linked terminal residues of N-acetyl-D-glucosamine. Immunochemistry. 1970 Oct;7(10):829–838. doi: 10.1016/0019-2791(70)90059-5. [DOI] [PubMed] [Google Scholar]
  35. Weigert M., Raschke W. C., Carson D., Cohn M. Immunochemical analysis of the idiotypes of mouse myeloma proteins with specificity for levan or dextran. J Exp Med. 1974 Jan 1;139(1):137–147. doi: 10.1084/jem.139.1.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Young N. M., Jocius I. B., Leon M. A. Binding properties of a mouse immunoglobulin M myeloma protein with carbohydrate specificity. Biochemistry. 1971 Aug 31;10(18):3457–3460. doi: 10.1021/bi00794a022. [DOI] [PubMed] [Google Scholar]

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

RESOURCES