Skip to main content
NCBI home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1964 Jan 1;119(1):1–19. doi: 10.1084/jem.119.1.1

THE FORMATION AND PROPERTIES OF POLIOVIRUS-NEUTRALIZING ANTIBODY

I. 19S AND 7S ANTIBODY FORMATION: DIFFERENCES IN KINETICS AND ANTIGEN DOSE REQUIREMENT FOR INDUCTION

Sven-Eric Svehag 1, Benjamin Mandel 1
PMCID: PMC2137811  PMID: 14113113

Abstract

Rapid formation of poliovirus-neutralizing antibody was observed in the rabbit. 19S type antibody was detectable 8 to 12 hours following a single intravenous virus injection and the induction period was of the order of 4 to 5 hours or less. The production of 7S antibody had a longer lag phase (1½ to 2 days) and it was formed at slower rate. The observed rate of early 19S and 7S antibody formation as well as the peak titers of the two antibodies were antigen dose dependent. Normal rabbit sera showed low neutralizing activity to several viral antigens in a sensitive assay system. Following intravenous inoculation of poliovirus either transitory (⩽ 1 month) or enduring (¾ to 1½ year) antibody formation resulted depending upon the dose of antigen employed. In transitory responses, which could be induced by a single small antigen dose, only 19S antibody was demonstrable and there was an abrupt cessation of antibody synthesis on day 4 or 5. In enduring responses, both 19S and 7S antibody were formed and the minimum antigen dose required for initiation of such a response was equal to the dose needed for induction of 7S antibody formation. Thus, enduring antibody formation was an all-or-none phenomenon depending upon whether or not 7S antibody formation was induced. The antigen dose requirement for induction of 7S antibody was much higher (by 50-fold or more) than that for 19S antibody. This allowed a determination of antigen dose regions, within which predictably transitory (19S) or enduring (19S + 7S) antibody formation was obtained. These pronounced differences in antigen dose requirement for induction and kinetics of formation of 19S and 7S antibody suggest that the same cells do not participate in the formation of the two antibodies.

Full Text

The Full Text of this article is available as a PDF (1,005.8 KB).

Selected References

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

  1. ASKONAS B. A., HUMPHREY J. H. Formation of specific antibodies and gamma-globulin in vitro; a study of the synthetic ability of various tissues from rabbits immunized by different methods. Biochem J. 1958 Feb;68(2):252–261. doi: 10.1042/bj0680252. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BANEY R. N., VAZQUEZ J. J., DIXON F. J. Cellular proliferation in relation to antibody synthesis. Proc Soc Exp Biol Med. 1962 Jan;109:1–4. doi: 10.3181/00379727-109-27083. [DOI] [PubMed] [Google Scholar]
  3. BENEDICT A. A., BROWN R. J., AYENGAR R. Physical properties of antibody to bovine serum albumin as demonstrated by hemagglutination. J Exp Med. 1962 Jan 1;115:195–208. doi: 10.1084/jem.115.1.195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BRADLEY S. G., WATSON D. W. PRODUCTION OF NEUTRALIZING ANTIBODY BY MICE INJECTED WITH ACTINOPHAGE. J Immunol. 1963 May;90:782–787. [PubMed] [Google Scholar]
  5. Bauer D. C., Stavitsky A. B. ON THE DIFFERENT MOLECULAR FORMS OF ANTIBODY SYNTHESIZED BY RABBITS DURING THE EARLY RESPONSE TO A SINGLE INJECTION OF PROTEIN AND CELLULAR ANTIGENS. Proc Natl Acad Sci U S A. 1961 Oct;47(10):1667–1680. doi: 10.1073/pnas.47.10.1667. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. DICK G. W. A., SCHWERDT C. E., HUBER W., SHARPLESS G. R., HOWE H. A. Immunization of cotton rats with inactivated Lansing poliomyelitis virus. II. Inactivation by physical methods. Am J Hyg. 1951 Mar;53(2):131–138. doi: 10.1093/oxfordjournals.aje.a119440. [DOI] [PubMed] [Google Scholar]
  7. DRAY S., YOUNG G. O. Differences in the antigenic components of sera of individual rabbits as shown by induced isoprecipitins. J Immunol. 1958 Aug;81(2):142–149. [PubMed] [Google Scholar]
  8. FAHEY J. L., GOODMAN H. C. Characterization of anti-thyroglobulin factors in human serum. J Clin Invest. 1960 Aug;39:1259–1265. doi: 10.1172/JCI104141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. GRUBB R., SWAHN B. Destruction of some agglutinins but not of others by two sulfhydryl compounds. Acta Pathol Microbiol Scand. 1958;43(3):305–309. doi: 10.1111/j.1699-0463.1958.tb04899.x. [DOI] [PubMed] [Google Scholar]
  10. GUNDERSON C. H., JURAS D., LA VIA M. F., WISSLER R. W. Tissue and cellular changes associated with antibody formation in the rat spleen. JAMA. 1962 Jun 23;180:1038–1047. [PubMed] [Google Scholar]
  11. HUMPHREY J. H., McFARLANE A. S. Rate of elimination of homologous globulins (including antibody) from the circulation. Biochem J. 1954 Jun;57(2):186–191. doi: 10.1042/bj0570186. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. JOHNSON A., WOERNLEY D., PRESSMAN D. Sedimentation properties of human and sheep erythrocyte hemolysins. J Immunol. 1957 Sep;79(3):234–237. [PubMed] [Google Scholar]
  13. LEDUC E. H., COONS A. H., CONNOLLY J. M. Studies on antibody production. II. The primary and secondary responses in the popliteal lymph node of the rabbit. J Exp Med. 1955 Jul 1;102(1):61–72. doi: 10.1084/jem.102.1.61. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. MANDEL B. Reversibility of the reaction between polio-virus and neutralizing antibody of rabbit origin. Virology. 1961 Jul;14:316–328. doi: 10.1016/0042-6822(61)90317-8. [DOI] [PubMed] [Google Scholar]
  16. NOSSAL G. J., MAKELA O. Autoradiographic studies on the immune response.I. The kinetics of plasma cell proliferation. J Exp Med. 1962 Jan 1;115:209–230. doi: 10.1084/jem.115.1.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. SCHOOLEY J. C. Autoradiographic observations of plasma cell formation. J Immunol. 1961 Mar;86:331–337. [PubMed] [Google Scholar]
  19. STELOS P., TALMAGE D. W. The separation by starch electrophoresis of two antibodies in sheep red cells differing in hemolytic efficiency. J Infect Dis. 1957 Mar-Apr;100(2):126–135. doi: 10.1093/infdis/100.2.126. [DOI] [PubMed] [Google Scholar]
  20. SVEHAG S. E., MANDEL B. THE FORMATION AND PROPERTIES OF POLIOVIRUS-NEUTRALIZING ANTIBODY. II. 19S AND 7S ANTIBODY FORMATION: DIFFERENCES IN ANTIGEN DOSE REQUIREMENT FOR SUSTAINED SYNTHESIS, ANAMNESIS, AND SENSITIVITY TO X-IRRADIATION. J Exp Med. 1964 Jan 1;119:21–39. doi: 10.1084/jem.119.1.21. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. SVEHAG S. E., MANDEL B. The production and properties of poliovirus neutralizing antibody of rabbit origin. Virology. 1962 Nov;18:508–510. doi: 10.1016/0042-6822(62)90050-8. [DOI] [PubMed] [Google Scholar]
  22. TALIAFERRO W. H., TALMAGE D. W. Antibodies in the rabbit with different rates of metabolic decay. J Infect Dis. 1956 Jul-Aug;99(1):21–33. doi: 10.1093/infdis/99.1.21. [DOI] [PubMed] [Google Scholar]
  23. THORBECKE G. J., ASOFSKY R. M., HOCHWALD G. M., SISKIND G. W. Gamma globulin and antibody formation in vitro. III. Induction of secondary response at different intervals after the primary; the role of secondary nodules in the preparation for the secondary response. J Exp Med. 1962 Sep 1;116:295–310. doi: 10.1084/jem.116.3.295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. UHR J. W., FINKELSTEIN M. S. Antibody formation. IV. Formation of rapidly and slowly sedimenting antibodies and immunological memory to bacteriophage phi-X 174. J Exp Med. 1963 Mar 1;117:457–477. doi: 10.1084/jem.117.3.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. UHR J. W., FINKELSTEIN M. S., BAUMANN J. B. Antibody formation. III. The primary and secondary antibody response to bacteriophage phi X 174 in guinea pigs. J Exp Med. 1962 Mar 1;115:655–670. doi: 10.1084/jem.115.3.655. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES