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The Chicken Yolk Sac IgY Receptor, a Functional Equivalent of the Mammalian MHC-Related Fc Receptor, Is a Phospholipase A_2 Receptor Homolog

机译:鸡卵囊IgY受体,与哺乳动物MHC相关的Fc受体的功能等效,是磷脂酶A_2受体的同源物

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摘要

In mammals, IgG is transferred from mother to young by the MHC-related receptor FcRn, which binds IgG in acidic endosomes and releases it at basic pH into blood. Maternal IgY, the avian counterpart of IgG, is transferred to embryos across yolk sac membranes. We affinity-purified the chicken yolk sac IgY receptor (FcRY) and sequenced its gene. FcRY is unrelated to MHC molecules but is a homolog of the mammalian phospholipase A_2 receptor. Analytical ultracentrifugation and truncation experiments suggest that FcRY forms a compact structure containing an IgY binding site at acidic pH but undergoes a conformational change at basic pH that disrupts the site. FcRY is thus unrelated to mammalian FcRn in both its structure and mechanism for pH-dependent binding, illustrating distinct routes utilized by evolution to transfer antibodies.
机译:在哺乳动物中,MHC相关受体FcRn将IgG从母亲转移到年轻,该受体结合酸性内体中的IgG,并在碱性pH值下释放到血液中。 IgG的禽类对应物母体IgY跨卵黄囊膜转移至胚胎。我们亲和纯化鸡卵囊IgY受体(FcRY),并对其基因进行测序。 FcRY与MHC分子无关,但是是哺乳动物磷脂酶A_2受体的同源物。分析性超速离心和截短实验表明,FcRY在酸性pH下形成一个包含IgY结合位点的致密结构,但在碱性pH下会发生构象变化,从而破坏该位点。因此,FcRY与哺乳动物FcRn的结构和pH依赖性结合机制均无关,这说明了进化过程中转移抗体所利用的独特途径。

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