ROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG
As assessed by decreased response of ConA-induced blasts to IL-2, a staphylococcal protein A was shown to extract IL-2 from cultural medium after its preincubation with IgG, but it did not bind pure IL-2. Normal human immunoglobulin inhibits reaction of DTH effectors to Listeria antigen, which is al...
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oai:doaj.org-article:68963ec2ee064950a8ad33e12da6f61c2021-11-18T08:03:37ZROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG1563-06252313-741X10.15789/1563-0625-2010-1-2-13-20https://doaj.org/article/68963ec2ee064950a8ad33e12da6f61c2014-07-01T00:00:00Zhttps://www.mimmun.ru/mimmun/article/view/33https://doaj.org/toc/1563-0625https://doaj.org/toc/2313-741XAs assessed by decreased response of ConA-induced blasts to IL-2, a staphylococcal protein A was shown to extract IL-2 from cultural medium after its preincubation with IgG, but it did not bind pure IL-2. Normal human immunoglobulin inhibits reaction of DTH effectors to Listeria antigen, which is also IL-2-dependent. An immunomodulating drug Phosprenyl (sodium polyprenylphosphate) abolishes the inhibitory ffect of immunoglobulin. Since Phosprenyl (as shown earlier) interacts with alpha-chain of rIL-2 and blocks IL-2 activity, the two drugs are in competitive relations. The latter may be explained by identities in prostetic carbohydrate groups of the both glycoproteins (CD25 and immunoglobulin), whereas Phosprenyl and IL-2 would behave like as lectins. These results characterize local conditions and mechanisms of immune regulation under tissue domination of gamma-globulin or antibodies of a given isotype. IgG binds with IL-2, reacting not with an active center but with effector region of IgG molecule, thus blocking IL-2 activity. Since a similar effect is observed under in vivo conditions (in a DTH model), the phenomenon revealed may explein inhibition of immune response after passive injection of antibodies, as well as a feed-back relationship between humoral and cellular immunity. Inhibition of IL-2 biological activity after its interaction with IgG and immune complexes may be considered as a universal mechanism of immune regulation performed by a feedback regulation, which may be influenced by means of Phosprenyl-like immunomodulators. In some infections, malignant growth etc., such mechanism may be of utmost pathogenetic significance. Moreover, such a mechanism cannot be also excluded in some physiological immunogenetic interactions, e.g., in feto-maternal system, where it could promote a positive selection for individuals with broader MHC repertoire, which would be necessary for development of individual and population-based resistance to infectionsS. M. SobolevT. N. NikolaevaE. A. GrigorjevaA. V. ProninSPb RAACIarticleil-2iggpolyprenolsimmunoregulationImmunologic diseases. AllergyRC581-607RUMedicinskaâ Immunologiâ, Vol 12, Iss 1-2, Pp 13-20 (2014) |
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il-2 igg polyprenols immunoregulation Immunologic diseases. Allergy RC581-607 |
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il-2 igg polyprenols immunoregulation Immunologic diseases. Allergy RC581-607 S. M. Sobolev T. N. Nikolaeva E. A. Grigorjeva A. V. Pronin ROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG |
description |
As assessed by decreased response of ConA-induced blasts to IL-2, a staphylococcal protein A was shown to extract IL-2 from cultural medium after its preincubation with IgG, but it did not bind pure IL-2. Normal human immunoglobulin inhibits reaction of DTH effectors to Listeria antigen, which is also IL-2-dependent. An immunomodulating drug Phosprenyl (sodium polyprenylphosphate) abolishes the inhibitory ffect of immunoglobulin. Since Phosprenyl (as shown earlier) interacts with alpha-chain of rIL-2 and blocks IL-2 activity, the two drugs are in competitive relations. The latter may be explained by identities in prostetic carbohydrate groups of the both glycoproteins (CD25 and immunoglobulin), whereas Phosprenyl and IL-2 would behave like as lectins. These results characterize local conditions and mechanisms of immune regulation under tissue domination of gamma-globulin or antibodies of a given isotype. IgG binds with IL-2, reacting not with an active center but with effector region of IgG molecule, thus blocking IL-2 activity. Since a similar effect is observed under in vivo conditions (in a DTH model), the phenomenon revealed may explein inhibition of immune response after passive injection of antibodies, as well as a feed-back relationship between humoral and cellular immunity. Inhibition of IL-2 biological activity after its interaction with IgG and immune complexes may be considered as a universal mechanism of immune regulation performed by a feedback regulation, which may be influenced by means of Phosprenyl-like immunomodulators. In some infections, malignant growth etc., such mechanism may be of utmost pathogenetic significance. Moreover, such a mechanism cannot be also excluded in some physiological immunogenetic interactions, e.g., in feto-maternal system, where it could promote a positive selection for individuals with broader MHC repertoire, which would be necessary for development of individual and population-based resistance to infections |
format |
article |
author |
S. M. Sobolev T. N. Nikolaeva E. A. Grigorjeva A. V. Pronin |
author_facet |
S. M. Sobolev T. N. Nikolaeva E. A. Grigorjeva A. V. Pronin |
author_sort |
S. M. Sobolev |
title |
ROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG |
title_short |
ROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG |
title_full |
ROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG |
title_fullStr |
ROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG |
title_full_unstemmed |
ROLE OF LECTIN-SUBSTRANCE RECOGNITION IN IMMUNOREGULATORY INTERACTION BETWEEN INTERLEUKIN-2 IGG |
title_sort |
role of lectin-substrance recognition in immunoregulatory interaction between interleukin-2 igg |
publisher |
SPb RAACI |
publishDate |
2014 |
url |
https://doaj.org/article/68963ec2ee064950a8ad33e12da6f61c |
work_keys_str_mv |
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_version_ |
1718422548259012608 |