NDLI: Polyreactivity of natural antibodies: Exchange by HL-fragments

Content Provider	Springer Nature Link
Author	Sedykh, M. A. Buneva, V. N. Nevinsky, G. A.
Copyright Year	2013
Abstract	The polyreactivity of binding (formation of antibody (AB) complexes not only with specific but also with foreign antigens) is a widespread phenomenon that in some cases can be caused by a conformational lability of the antigen-binding sites of antibodies (which increases upon treatment with various destabilizing agents) and leads to AB binding with very different antigens. Some ABs exist as dimers of the initial ABs and their idiotypes (or anti-idiotypes) capable of producing intramolecular cyclic complexes with features of polyreactants. Another mechanism of binding polyreactivity is an exchange in blood by halves of IgG4 molecules (HL-fragments) against various antigens. Also, for the first time catalytic polyfunctionality of human milk ABs has been detected, which is caused by an exchange by HL-fragments between molecules of λ- and κ-IgG (IgG1-IgG4) and also by λ- and κ-sIgA against different antigens with formation of very different chimeric antibodies. This review considers all possible pathways of formation of polyspecific immunoglobulins and their biological functions described in the literature, as well as mechanisms of binding polyreactivity and catalytic polyfunctionality of natural antibodies.
Starting Page	1305
Ending Page	1320
Page Count	16
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	78
Issue Number	12
e-ISSN	16083040
Language	English
Publisher	Pleiades Publishing
Publisher Date	2013-12-17
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	antibodies natural abzymes polyreactivity of binding catalytic polyfuctionality Biochemistry Bioorganic Chemistry Microbiology Biomedicine general
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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