STRUCTURE AND BINDING-PROPERTIES OF MONOCLONAL-ANTIBODIES TO CORE HISTONES FROM AUTOIMMUNE MICE

Citation
M. Monestier et al., STRUCTURE AND BINDING-PROPERTIES OF MONOCLONAL-ANTIBODIES TO CORE HISTONES FROM AUTOIMMUNE MICE, Molecular immunology, 30(12), 1993, pp. 1069-1075
Citations number
36
Categorie Soggetti
Immunology,Biology
Journal title
ISSN journal
01615890
Volume
30
Issue
12
Year of publication
1993
Pages
1069 - 1075
Database
ISI
SICI code
0161-5890(1993)30:12<1069:SABOMT>2.0.ZU;2-T
Abstract
Histones are frequent targets of self-reactive antibodies during autoi mmune syndromes. We report the specificities and V region genes of thr ee IgG anti-histone MAbs obtained from autoimmune mice. Each of the MA bs, named LG2-1, LG2-2 and BWA3, is directed against a different deter minant located in the basic amino-terminal domain of core histones LG2 -1 reacts a peptide from histone H3 (residues 30-45), LG2-2 recognizes the amino-terminus of H2B (residues 1-13) and BWA3 binds an epitope c orresponding to a region of high sequence similarity between H2A and H 4 (residues 1-20 and 1-29, respectively). The analysis of their V regi on sequences indicates that the H chain CDRs of these MAbs are remarka ble for the presence of negatively charged amino acid residues that ma y play a role in the binding to cationic histones. The H chain importa nce in conferring reactivity to histones is corroborated by the observ ation that each of the V(H) gene segments of these MAbs is very simila r to V(H) genes of previously described murine anti-histone antibodies .