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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1982 Feb;79(4):1277–1281. doi: 10.1073/pnas.79.4.1277

Monoclonal IgM radioimmunoassay for hepatitis B surface antigen: high binding activity in serum that is unreactive with conventional antibodies.

J R Wands, R R Bruns, R I Carlson, A Ware, J E Menitove, K J Isselbacher
PMCID: PMC345945  PMID: 6951173

Abstract

Using a monoclonal IgM antibody (anti-HBs) to hepatitis B surface antigen (HBsAg) in a radioimmunoassay for hepatitis B, we have detected high binding activity in human serum that was unreactive in assays employing conventional anti-HBs reagents. The binding material was isolated from serum by affinity chromatography on monoclonal IgM anti-HBs, and comparison of the material with HBsAg (by sodium dodecyl sulfate/polyacrylamide gel electrophoresis) demonstrated that the two shared several similar polypeptides. Furthermore, comparison of the binding properties of HBsAg and concentrated monoclonal immunoreactive material with conventional and monoclonal anti-HBs reagents demonstrated some antigenic crossreactivity. The molecular weight of the monoclonal immunoreactive material was approximately 2 X 10(6). Immunoprecipitation of the material with monoclonal IgM antibodies and examination by electron microscopy revealed clumped and "spiculated" particles that resembled 22-nm hepatitis B particles coated with the same antibody. Thus, this study suggests that the high-binding-activity material, detected in serum only by the monoclonal radioimmunoassay, is not identical with HBsAg, but it shares some common properties.

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Selected References

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  1. Dienstag J. L., Rhodes A. R., Bhan A. K., Dvorak A. M., Mihm M. C., Jr, Wands J. R. Urticaria associated with acute viral hepatitis type B: studies of pathogenesis. Ann Intern Med. 1978 Jul;89(1):34–40. doi: 10.7326/0003-4819-89-1-34. [DOI] [PubMed] [Google Scholar]
  2. Feinstone S. M., Kapikian A. Z., Purceli R. H. Hepatitis A: detection by immune electron microscopy of a viruslike antigen associated with acute illness. Science. 1973 Dec 7;182(4116):1026–1028. doi: 10.1126/science.182.4116.1026. [DOI] [PubMed] [Google Scholar]
  3. Mishiro S., Imai M., Takahashi K., Machida A., Gotanda T., Miyakawa Y., Mayumi M. A 49,000-dalton polypeptide bearing all antigenic determinants and full immunogenicity of 22-nm hepatitis B surface antigen particles. J Immunol. 1980 Apr;124(4):1589–1593. [PubMed] [Google Scholar]
  4. Moriarty A. M., Hoyer B. H., Shih J. W., Gerin J. L., Hamer D. H. Expression of the hepatitis B virus surface antigen gene in cell culture by using a simian virus 40 vector. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2606–2610. doi: 10.1073/pnas.78.4.2606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Shouval D., Wands J. R., Zurawski V. R., Jr, Isselbacher K. J., Shafritz D. A. Selecting binding and complement-mediated lysis of human hepatoma cells (PLC/PRF/5) in culture by monoclonal antibodies to hepatitis B surface antigen. Proc Natl Acad Sci U S A. 1982 Jan;79(2):650–654. doi: 10.1073/pnas.79.2.650. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Wands J. R., Carlson R. I., Schoemaker H., Isselbacher K. J., Zurawski V. R., Jr Immunodiagnosis of hepatitis B with high-affinity IgM monoclonal antibodies. Proc Natl Acad Sci U S A. 1981 Feb;78(2):1214–1218. doi: 10.1073/pnas.78.2.1214. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Wands J. R., Chura C. M., Roll F. J., Maddrey W. C. Serial studies of hepatitis-associated antigen and antibody in patients receiving antitumor chemotherapy for myeloproliferative and lymphoproliferative disorders. Gastroenterology. 1975 Jan;68(1):105–112. [PubMed] [Google Scholar]
  8. Wands J. R., Zurawski V. R., Jr High affinity monoclonal antibodies to hepatitis B surface antigen (HBsAg) produced by somatic cell hybrids. Gastroenterology. 1981 Feb;80(2):225–232. [PubMed] [Google Scholar]
  9. Williams A. F., Galfrè G., Milstein C. Analysis of cell surfaces by xenogeneic myeloma-hybrid antibodies: differentiation antigens of rat lymphocytes. Cell. 1977 Nov;12(3):663–673. doi: 10.1016/0092-8674(77)90266-5. [DOI] [PubMed] [Google Scholar]

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