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. 1980 Oct 1;152(4):979–995. doi: 10.1084/jem.152.4.979

Human monoclonal macroglobulins with specificity for Klebsiella K polysaccharides that contain 3,4-pyruvylated-D-galactose and 4,6- pyruvylated-D-galactose

PMCID: PMC2185977  PMID: 6158553

Abstract

Two human IgM myeloma proteins, IgMWEA and IgMMAY, were found to react with agar and Klebsiella polysaccharides that contain pyruvylated D- galactose (DGal). Quantitative precipitin data and precipitin inhibition studies with methyl alpha- and beta-glycosides of 4,6- pyruvylated-D-galactose showed their combining sites to be different, although each was directed against the pyruvylated-D-Gal, one reacting most specifically with Klebsiella polysaccharides with terminal nonreducing beta-linked 2,4 pyruvylated-D-Gal, whereas the other reacted equally well with Klebsiella polysaccharides that contain 3,4 beta-linked and 4,6 alpha-linked terminal nonreducing pyruvylated-DGal. Inhibition studies showed that both sites are directed toward one of the two space isomers of 3,4- or 4,6-pyruvylated DGal, the form in which the methyl group of the pyruvate is equatorial, or endo, and its carboxyl group axial, or exo, to the plane of the acetal ring. Coprecipitation studies showed the combining site of IgMWEA to be located on an (Fab')2 fragment and not on the (Fc)5mu fragment. The monoclonal peak in the serum of IgMMAY was specifically precipitated by Klebsiella polysaccharide. Myeloma proteins with specificities of this type may occur with reasonable frequency in humans and may be a consequence of clonal expansion from inapparent infection, carrier states, or disease produced by various Klebsiella organisms.

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Selected References

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  1. Alving C. R., Joseph K. C., Wistar R. Influence of membrane composition on the interaction of a human monoclonal "anti-Forssman" immunoglobulin with liposomes. Biochemistry. 1974 Nov 5;13(23):4818–4824. doi: 10.1021/bi00720a021. [DOI] [PubMed] [Google Scholar]
  2. Bhavanandan V. P., Meyer K. Studies on keratosulfates. Methylation, desulfation, and acid hydrolysis studies on old human rib cartilage keratosulfate. J Biol Chem. 1968 Mar 10;243(5):1052–1059. [PubMed] [Google Scholar]
  3. Chaudhari A. S., Bishop C. T., Dudman W. F. Structural studies on the specific capsular polysaccharide from Rhizobium trifolii, TA-1. Carbohydr Res. 1973 Jun;28(2):221–231. doi: 10.1016/s0008-6215(00)82778-0. [DOI] [PubMed] [Google Scholar]
  4. Corash L. M., Piomelli S., Chen H. C., Seaman C., Gross E. Separation of erythrocytes according to age on a simplified density gradient. J Lab Clin Med. 1974 Jul;84(1):147–151. [PubMed] [Google Scholar]
  5. Feizi T., Kabat E. A. Immunochemical studies on blood groups. LIV. Classification of anti-I and anti-i sera into groups based on reactivity patterns with various antigens related to the blood group A,B,H, Le a, Le b and precursor substances. J Exp Med. 1972 Jun 1;135(6):1247–1258. doi: 10.1084/jem.135.6.1247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Feizi T., Kabat E. A., Vicari G., Anderson B., Marsh W. L. Immunochemical studies on blood groups.XLIX. The I antigen complex: specificity differences among anti-I sera revealed by quantitative precipitin studies; partial structure of the I determinant specific for one anti-I serum. J Immunol. 1971 Jun;106(6):1578–1592. [PubMed] [Google Scholar]
  7. Freedman M., Merrett R., Pruzanski W. Human monoclonal immunoglobulins with antibody-like activity. Immunochemistry. 1976 Mar;13(3):193–202. doi: 10.1016/0019-2791(76)90215-9. [DOI] [PubMed] [Google Scholar]
  8. Hannestad K., Eriksen J., Christensen T., Harboe M. Multiple M-components in a single individual. I. The structural relationship of two serum gamma M kappa M-components as revealed by combining specificity and individual antigenic specificity. Immunochemistry. 1970 Nov;7(11):899–915. [PubMed] [Google Scholar]
  9. Hannestad K., Sletten K. Multiple M-components in a single individual. 3. Heterogeneity of M-components in two macroglobulinemia sera with anti-polysaccharide activity. J Biol Chem. 1971 Nov 25;246(22):6982–6990. [PubMed] [Google Scholar]
  10. Heidelberger M., Kvarnström I., Eriksen J., Nimmich W., Dudman W. F. Immunochemical determination of the configuration of a haptenic substituent. Proc Natl Acad Sci U S A. 1980 Jul;77(7):4244–4246. doi: 10.1073/pnas.77.7.4244. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Heidelberger M., Macpherson C. F. QUANTITATIVE MICRO-ESTIMATION OF ANTIBODIES IN THE SERA OF MAN AND OTHER ANIMALS. Science. 1943 Apr 30;97(2522):405–406. doi: 10.1126/science.97.2522.405. [DOI] [PubMed] [Google Scholar]
  12. Higginbotham J. D., Heidelberger M. Oxidation of the capsular polysaccharide of pneumococcal type IV by periodate. Carbohydr Res. 1973 Apr;27(2):297–302. doi: 10.1016/s0008-6215(00)81312-9. [DOI] [PubMed] [Google Scholar]
  13. Higginbotham J. D., Heidelberger M. The specific capsular polysaccharide of Pneumococcus type IV. Carbohydr Res. 1972 Jul;23(2):165–173. doi: 10.1016/s0008-6215(00)88021-0. [DOI] [PubMed] [Google Scholar]
  14. Lew J. Y., Heidelberger M. Linkage of pyruvyl groups in the specific capsular polysaccharide of Pneumococcus type IV. Carbohydr Res. 1976 Dec;52:255–258. doi: 10.1016/s0008-6215(00)85971-6. [DOI] [PubMed] [Google Scholar]
  15. Lindberg B., Lindh F., Lönngren J., Nimmich W. Structural studies of the capsular polysaccharide of Klebsiella type 33. Carbohydr Res. 1979 Apr;70(1):135–144. doi: 10.1016/s0008-6215(00)83277-2. [DOI] [PubMed] [Google Scholar]
  16. Lindberg B., Lindh F., Lönngren J., Sutherland I. W. Structural studies of the capsular polysaccharide of Klebsiella type 30. Carbohydr Res. 1979 Nov;76:281–284. doi: 10.1016/0008-6215(79)80031-2. [DOI] [PubMed] [Google Scholar]
  17. MAY F., WEINLAND H. Beobachtungen bei der Säurehydrolyse des Galaktogens. III. Nachweis der beta-D-1-3-Bindung als Hauptkettenbindung in Tri- und Pentasacchariden. Hoppe Seylers Z Physiol Chem. 1956 Sep 25;305(4-6):207–218. [PubMed] [Google Scholar]
  18. Miller F., Metzger H. Characterization of a human macroglobulin. 3. The products of tryptic digestion. J Biol Chem. 1966 Apr 25;241(8):1732–1740. [PubMed] [Google Scholar]
  19. Naiki M., Marcus D. M. Binding of N-acetylgalactosamine-containing compounds by a human IgM paraprotein. J Immunol. 1977 Aug;119(2):537–539. [PubMed] [Google Scholar]
  20. Plaut A. G., Tomasi T. B., Jr Immunoglobulin M: pentameric Fcmu fragments released by trypsin at higher temperatures. Proc Natl Acad Sci U S A. 1970 Feb;65(2):318–322. doi: 10.1073/pnas.65.2.318. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Potter M. Antigen-binding myeloma proteins of mice. Adv Immunol. 1977;25:141–211. [PubMed] [Google Scholar]
  22. Potter M. Experimental approaches to homogenous antibody populations. Mouse IgA myeloma proteins that bind polysaccharide antigens of enterobacterial origin. Fed Proc. 1970 Jan-Feb;29(1):85–91. [PubMed] [Google Scholar]
  23. 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]
  24. Riesen W., Rudikoff S., Oriol R., Potter M. An IgM Waldenström with specificity against phosphorylcholine. Biochemistry. 1975 Mar 11;14(5):1052–1057. doi: 10.1021/bi00676a026. [DOI] [PubMed] [Google Scholar]
  25. Roelcke D. Cold agglutination. Antibodies and antigens. Clin Immunol Immunopathol. 1974 Jan;2(2):266–280. doi: 10.1016/0090-1229(74)90044-0. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. Seligmann M., Brouet J. C. Antibody activity of human myeloma globulins. Semin Hematol. 1973 Apr;10(2):163–177. [PubMed] [Google Scholar]
  28. Tiselius A., Kabat E. A. AN ELECTROPHORETIC STUDY OF IMMUNE SERA AND PURIFIED ANTIBODY PREPARATIONS. J Exp Med. 1939 Jan 1;69(1):119–131. doi: 10.1084/jem.69.1.119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Tsai C. M., Zopf D. A., Wistar R., Jr, Ginsburg V. A human cold agglutinin which binds lacto-N-neotetraose. J Immunol. 1976 Sep;117(3):717–721. [PubMed] [Google Scholar]
  30. Tsai C. M., Zopf D. A., Yu R. K., Wistar R., Jr, Ginsburg V. A Waldenström macroglobulin that is both a cold agglutinin and a cryoglobulin because it binds N-acetylneuraminosyl residues. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4591–4594. doi: 10.1073/pnas.74.10.4591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Vicari G., Kabat E. A. Immunochemical studies on blood groups. XLII. Isolation and characterization from ovarian cyst fluid of a blood group substance lacking A, B, H, Lea and Leb specificity. J Immunol. 1969 Apr;102(4):821–825. [PubMed] [Google Scholar]
  32. WEINLAND H. Beobachtungen bei der Säurehydrolyse des Galaktogens. V. Die säurestabilen Phosphorsäureester. Galaktose-6-phosphorsäure, frei, und als Bestandteil einer Trisaccharid-monophosphorsäure. Hoppe Seylers Z Physiol Chem. 1956 Dec 10;306(2-3):56–65. [PubMed] [Google Scholar]
  33. Yoo T. J., Franklin E. C. Lack of antibody activity in human myeloma proteins. J Immunol. 1971 Aug;107(2):365–367. [PubMed] [Google Scholar]

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