The structure and origin of rheumatoid factors

被引：74

作者：

Sutton, B

Corper, A

Bonagura, V

Taussig, M

机构：

[1] Kings Coll London, Randall Ctr, London SE1 1UL, England

[2] Long Isl Jewish Med Ctr, Schneider Childrens Hosp, Dept Pediat, New Hyde Pk, NY 11040 USA

[3] Babraham Inst, Lab Mol Recognit, Cambridge CB2 4AT, England

来源：

IMMUNOLOGY TODAY | 2000年 / 21卷 / 04期

关键词：

D O I：

10.1016/S0167-5699(00)01589-9

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

The recently determined X-ray crystal structure of a human rheumatoid factor Fab bound to IgG Fe provides the basis of a new hypothesis for the origin of these autoantibodies in rheumatoid arthritis. The observation that Fe is bound outside the conventional antigen combining site suggests it novel form of crossreactivity with simultaneous binding of another antigen, potentiated by somatic mutation. This article discusses the implications for the induction of these autoantibodies.

引用

页码：177 / 183

页数：7

共 47 条

[31]

RANDEN I, 1992, J IMMUNOL, V148, P3296

[32] EFFICIENT AND SELECTIVE PRESENTATION OF ANTIGEN-ANTIBODY COMPLEXES BY RHEUMATOID-FACTOR B-CELLS [J].