Ukr.Biochem.J. 2015; Volume 87, Issue 5, Sep-Oct, pp. 46-53


Fundamental differences between natural antibodies and polyreactive immunoglobulins

S. A. Bobrovnik, M. A. Demchenko, S. V. Komisarenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;

A problem of similarity and differences between so-called polyreactive immunoglobulins (PRIGs) and natural antibodies (NAbs), capable of cross-reacting with some structurally dissimilar antigens, has been considered. The analysis of mechanisms of an unspecific interaction between PRIGs or NAbs and antigens evidences for the fact that essential differences exist between these substances. These differences permit classifying the abovementioned substances as different types of immunoglobulin molecules. The major difference between PRIGs and NAbs may include both the mechanisms of the above mentioned immunoglobulin molecules binding to antigens and their interaction affinity, as well as an absolutely different influence of some low-molecular substances on the efficiency of the interaction with antigens. Relying on the obtained data it can be assumed that, since PRIGs and NAbs have fundamental differences, they may perform not only similar but also different functions of the immune system.

Keywords: , , ,


  1. Bobrovnik SA. Activation of “silent” antibodies and their interaction with antigens.  Ukr Biokhim Zhurn. 1990 Sep-Oct;62(5):86-9. Russian. PubMed
  2. Avrameas S, Guilbert B, Dighiero G. Natural antibodies against tubulin, actin myoglobin, thyroglobulin, fetuin, albumin and transferrin are present in normal human sera, and monoclonal immunoglobulins from multiple myeloma and Waldenström’s macroglobulinemia may express similar antibody specificities  Ann Immunol (Paris). 1981 Mar-Apr;132C(2):231-6. PubMed, CrossRef
  3. Guilbert B, Dighiero G, Avrameas S. Naturally occurring antibodies against nine common antigens in human sera. I. Detection, isolation and characterization. J Immunol. 1982 Jun;128(6):2779-87. PubMed
  4. Dighiero G, Guilbert B, Avrameas S. Naturally occurring antibodies against nine common antigens in humans sera. II. High incidence of monoclonal Ig exhibiting antibody activity against actin and tubulin and sharing antibody specificities with natural antibodies. J Immunol. 1982 Jun;128(6):2788-92. PubMed
  5. Avrameas S. Natural autoantibodies: from ‘horror autotoxicus’ to ‘gnothi seauton’. Immunol Today. 1991 May;12(5):154-9. Review. PubMed, CrossRef
  6. Avrameas S, Ternynck T. The natural autoantibodies system: between hypotheses and facts. Mol Immunol. 1993 Aug;30(12):1133-42. Review. PubMed, CrossRef
  7. Bobrovnik SA, Starodub NF. A new simple method of antigen immobilization on immunological plates. Immunology (Moscow). 1988;(5):83-85. Russian.
  8. Bobrovnik SA. Polyreactive immunoglobulins recognize hydrophobic parts of proteins. Ukr Biokhim Zhurn. 2001 Mar-Apr;73(2):116-22. Russian. PubMed
  9. Bobrovnik SA. Polyreactive immunoglobulins: molecular properties and functions. Comments Mol Cell Biophys. 1999;9:323-356.
  10. Friguet B, Chaffotte AF, Djavadi-Ohaniance L, Goldberg ME. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J Immunol Methods. 1985 Mar 18;77(2):305-19. PubMed, CrossRef
  11. Stevens FJ. Modification of an ELISA-based procedure for affinity determination: correction necessary for use with bivalent antibody. Mol Immunol. 1987 Oct;24(10):1055-60. PubMed, CrossRef
  12. Bobrovnik SA. Avidity of polyreactive immunoglobulins. Ukr Biochem J. 2014 Nov-Dec;86(6):183-9. Russian. PubMed, CrossRef
  13. Bobrovnik SA, Lavrenchuk GI, Benkovska NP, Chornaya NE. Influence of polyreactive immunoglobulins on tumor cells prolipheration. Exp Oncol. 1998;(20):202-207. (In Russian).

Creative CommonsThis work is licensed under a Creative Commons Attribution 4.0 International License.