Skip to main content
NCBI home page
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
. 1981 Feb;78(2):1214–1218. doi: 10.1073/pnas.78.2.1214

Immunodiagnosis of hepatitis B with high-affinity IgM monoclonal antibodies.

J R Wands, R I Carlson, H Schoemaker, K J Isselbacher, V R Zurawski Jr
PMCID: PMC319978  PMID: 6940137

Abstract

High-affinity monoclonal IgG and IgM antibodies to hepatitis B surface antigen (HBsAg) have been prepared and their functional capabilities explored by means of solid-phase radioimmunoassays. 125I-labeled HBsAg binding studies indicated that monoclonal IgM antibodies against HBsAg (anti-HBs) coupled to a solid-phase support quantitatively bound more HbsAg at a faster rate than conventionally prepared anti-HBs reagents or other high-affinity IgG monoclonal anti-HBs antibodies. Consequently, IgM anti-HBs was also radiolabeled, and an IgM-IgM radioimmunoassay was developed for the immunodiagnosis of hepatitis B. The lower limit of this assay was approximately 100 pg +/- 30 (SEM) of HBsAg per ml of serum. Compared to available commercial radioassays, preliminary studies have shown the IgM-IgM assay to have increased sensitivity, which improved the detection of a HBsAg-associated determinant in acute hepatitis and post transfusion hepatitis. It is probable that the multivalent interaction between monoclonal IgM anti-HBs and the polydeterminant HBsAg is important in augmenting the performance of this monoclonal assay.

Full text

PDF
1214

Selected References

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

  1. BLUMBERG B. S. POLYMORPHISMS OF THE SERUM PROTEINS AND THE DEVELOPMENT OF ISO-PRECIPITINS IN TRANSFUSED PATIENTS. Bull N Y Acad Med. 1964 May;40:377–386. [PMC free article] [PubMed] [Google Scholar]
  2. Blank S. E., Leslie G. A., Clem L. W. Antibody affinity and valence in viral neutralization. J Immunol. 1972 Mar;108(3):665–673. [PubMed] [Google Scholar]
  3. Bolton A. E., Hunter W. M. The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Biochem J. 1973 Jul;133(3):529–539. doi: 10.1042/bj1330529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Crothers D. M., Metzger H. The influence of polyvalency on the binding properties of antibodies. Immunochemistry. 1972 Mar;9(3):341–357. doi: 10.1016/0019-2791(72)90097-3. [DOI] [PubMed] [Google Scholar]
  5. Dane D. S., Cameron C. H., Briggs M. Virus-like particles in serum of patients with Australia-antigen-associated hepatitis. Lancet. 1970 Apr 4;1(7649):695–698. doi: 10.1016/s0140-6736(70)90926-8. [DOI] [PubMed] [Google Scholar]
  6. Dreesman G. R., Hollinger F. B., Suriano J. R., Fujioka R. S., Brunschwig J. P., Melnick J. L. Biophysical and biochemical heterogeneity of purified hepatitis B antigen. J Virol. 1972 Sep;10(3):469–476. doi: 10.1128/jvi.10.3.469-476.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ehrlich P. H. The effect of multivalency on the specificity of protein and cell interactions. J Theor Biol. 1979 Nov 7;81(1):123–127. doi: 10.1016/0022-5193(79)90085-7. [DOI] [PubMed] [Google Scholar]
  8. Hoofnagle J. H., Seeff L. B., Bales Z. B., Zimmerman H. J. Type B hepatitis after transfusion with blood containing antibody to hepatitis B core antigen. N Engl J Med. 1978 Jun 22;298(25):1379–1383. doi: 10.1056/NEJM197806222982502. [DOI] [PubMed] [Google Scholar]
  9. Köhler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975 Aug 7;256(5517):495–497. doi: 10.1038/256495a0. [DOI] [PubMed] [Google Scholar]
  10. Köhler G., Milstein C. Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion. Eur J Immunol. 1976 Jul;6(7):511–519. doi: 10.1002/eji.1830060713. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Marchalonis J. J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem J. 1969 Jun;113(2):299–305. doi: 10.1042/bj1130299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Marshak-Rothstein A., Fink P., Gridley T., Raulet D. H., Bevan M. J., Gefter M. L. Properties and applications of monoclonal antibodies directed against determinants of the Thy-1 locus. J Immunol. 1979 Jun;122(6):2491–2497. [PubMed] [Google Scholar]
  14. Metzger H. Structure and function of gamma M macroglobulins. Adv Immunol. 1970;12:57–116. doi: 10.1016/s0065-2776(08)60168-6. [DOI] [PubMed] [Google Scholar]
  15. Mosley J. W., Redeker A. G., Feinstone S. M., Purcell R. H. Mutliple hepatitis viruses in multiple attacks of acute viral hepatitis. N Engl J Med. 1977 Jan 13;296(2):75–78. doi: 10.1056/NEJM197701132960204. [DOI] [PubMed] [Google Scholar]
  16. Prince A. M. An antigen detected in the blood during the incubation period of serum hepatitis. Proc Natl Acad Sci U S A. 1968 Jul;60(3):814–821. doi: 10.1073/pnas.60.3.814. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Takahashi K., Akahane Y., Gotanda T., Mishiro T., Imai M., Miyakawa Y., Mayumi M. Demonstration of hepatitis B e antigen in the core of Dane particles. J Immunol. 1979 Jan;122(1):275–279. [PubMed] [Google Scholar]
  18. 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]
  19. 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]
  20. 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]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES