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Detection and characterization of B cell epitopes on beta2-glycoprotein I.

机译:β2-糖蛋白I上B细胞表位的检测和表征。

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摘要

Autoantibodies in antiphospholipid syndrome react predominantly with the plasma protein beta2-glycoprotein I (beta2GPI). Work by a large number of investigators has led to considerable progress in detecting and understanding beta2GPI reactivity with autoantibodies. Characterization of B cell epitopes on beta2GPI has benefited from an appreciation of its interactions with anionic phospholipids and a variety of microplate surfaces. In particular, autoantibodies to beta2GPI are of sufficiently low affinity to require high concentrations of antigen for detectable reactivity. Moreover, some microplate surfaces do not support the proper orientation of beta2GPI to allow display of epitopes in a manner accessible to autoantibodies. These concepts have helped to explain previous notions that exposure of cryptic beta2GPI epitopes may require interactions with anionic surfaces. Finally, we review evidence identifying a dominant B cell epitope that is partially defined by residues Gly40 and Arg43 on the amino terminal domain of beta2GPI.
机译:抗磷脂综合征中的自身抗体主要与血浆蛋白β2-糖蛋白I(β2GPI)反应。大量研究人员的工作已导致在检测和了解β2GPI与自身抗体的反应性方面取得了长足的进步。 beta2GPI上B细胞表位的表征得益于其与阴离子磷脂和各种微孔板表面相互作用的认识。特别地,针对β2GPI的自身抗体具有足够低的亲和力,从而需要高浓度的抗原以用于可检测的反应性。此外,一些微孔板表面不支持beta2GPI的正确方向,以允许以自身抗体可及的方式展示表位。这些概念有助于解释先前的观念,即隐匿的beta2GPI表位的暴露可能需要与阴离子表面相互作用。最后,我们审查了鉴定占主导地位的B细胞表位的证据,该表位部分由beta2GPI氨基末端域上的残基Gly40和Arg43定义。

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