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The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction

机译:支原体表面蛋白质MIB和MIP促进抗体 - 抗原相互作用的解离

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Mycoplasma immunoglobulin binding (MIB) and mycoplasma immunoglobulin protease (MIP) are surface proteins found in the majority of mycoplasma species, acting sequentially to capture antibodies and cleave off their V H domains. Cryo–electron microscopy structures show how MIB and MIP bind to a Fab fragment in a “hug of death” mechanism. As a result, the orientation of the V L and V H domains is twisted out of alignment, disrupting the antigen binding site. We also show that MIB-MIP has the ability to promote the dissociation of the antibody-antigen complex. This system is functional in cells and protects mycoplasmas from antibody-mediated agglutination. These results highlight the key role of the MIB-MIP system in immunity evasion by mycoplasmas through an unprecedented mechanism, and open exciting perspectives to use these proteins as potential tools in the antibody field.
机译:支原体免疫球蛋白结合(MIB)和支原体免疫球蛋白蛋白酶(MIP)是在大部分支原体物种中发现的表面蛋白,依次作用以捕获抗体并切断其V H结构域。 冷冻电子显微镜结构显示MIB和MIP如何在“死亡中的拥抱”机制中与Fab片段结合。 结果,Vl和V H结构域的取向被取出取向,破坏抗原结合位点。 我们还表明,MIB-MIP能够促进抗体 - 抗原复合物的解离。 该系统在细胞中具有功能性,并保护支原体免受抗体介导的凝集凝集。 这些结果突出了MIB-MIP系统通过前所未有的机制通过前所未有的机制来突出的MIB-MIP系统的关键作用,并打开令人兴奋的观点来使用这些蛋白质作为抗体场中的潜在工具。

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