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Mechanisms of interaction of polyreactive immunoglobulins and protein antigens

Bobrovnik, S.A.

Ukrains'kyi Biokhimichnyi Zhurnal 74(2): 37-44

2002

ISSN/ISBN: 0372-3909
PMID: 12152311
Document Number: 543923
New features of interaction between polyreactive immunoglobulins (PRIG) and protein antigens were considered. It was shown that unlike specific antibodies, recognizing mainly hydrophilic epitops of proteins and interacting against them with high affinity according to the mechanisms "lock-and-key" and/or "induced fit", PRIG recognized and nonspecifically bound to hydrophobic patches of protein antigens. On this reason it is possible to prevent or markedly diminish PRIG-antigen interaction using the reagents that have high affinity to hydrophobic regions of proteins and therefore are capable to block these regions. The obtained data are in a good agreement with the former data concerning the kinetic and thermodynamics characteristics of PRIG-antigen interaction described by us earlier.

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