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首页> 外文期刊>Infection and immunity >Structural and Functional Consequences of Cleavage of Human Secretory and Human Serum Immunoglobulin A1 by Proteinases from Proteus mirabilis and Neisseria meningitidis
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Structural and Functional Consequences of Cleavage of Human Secretory and Human Serum Immunoglobulin A1 by Proteinases from Proteus mirabilis and Neisseria meningitidis

机译：变形杆菌和脑膜炎奈瑟氏球菌蛋白酶切割人分泌物和人血清免疫球蛋白A1的结构和功能后果。

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The cleavage of human serum monomeric immunoglobulin A1 (IgA1) and human secretory IgA1 (S-IgA1) by IgA1 proteinase of Neisseria meningitidis and cleavage by the proteinase from Proteus mirabilis have been compared. For serum IgA1, both proteinases cleaved only the α chain. N. meningitidis proteinase cleaved only in the hinge. P. mirabilis proteinase sequentially removed the tailpiece, the CH3 domain, and the CH2 domain. The cleavage of S-IgA1 by N. meningitidis proteinase occurred only in the hinge and was as rapid as that of serum IgA1. P. mirabilis proteinase predominantly cleaved the secretory component (SC) of S-IgA1. The SC of S-IgA1, whether cleaved or not, appeared to protect the α1 chain. Purified Fc fragment derived from the cleavage of serum IgA1 by N. meningitidis proteinase stimulated a respiratory burst in neutrophils through Fcα receptors, whereas the (Fcα1)2-SC fragment from digested S-IgA1 did not. The loss of the tailpiece from serum IgA1 treated with P. mirabilis proteinase had little effect, but the loss of the CH3 domain was concurrent with a rapid loss in the ability to bind to Fcα receptors. S-IgA1 treated with P. mirabilis proteinase under the same conditions retained the ability to bind to Fcα receptors. The results are consistent with the Fcα receptor binding site being at the CH2-CH3 interface. These data shed further light on the structure of S-IgA1 and indicate that the binding site for the Fcα receptor in S-IgA is protected by SC, thus prolonging its ability to activate phagocytic cells at the mucosal surface.
机译：奈瑟氏菌 脑膜炎双球菌的IgA1蛋白酶对人血清单体免疫球蛋白A1（IgA1）和人分泌型IgA1（S-IgA1）的裂解，以及 Proteus的蛋白酶对人血清免疫球蛋白A1的裂解 奇迹已被比较。对于血清IgA1，两种蛋白酶均仅裂解α链。 N 。 meningitidis 蛋白酶仅在铰链处切割。 P 。 mirabilis 蛋白酶顺序去除了尾部，CH3结构域和CH2结构域。 S-IgA1被 N 切割。 meningitidis 蛋白酶仅在铰链中发生，并且与血清IgA1一样快。 P 。 mirabilis 蛋白酶主要切割S-IgA1的分泌成分（SC）。 S-IgA1的SC，无论是否断裂，似乎都可以保护α1链。通过 N 切割血清IgA1产生的纯化Fc片段。 脑膜炎蛋白酶通过Fcα受体刺激中性粒细胞呼吸爆发，而消化的S-IgA1的（Fcα1） 2 -SC片段则没有。用 P 处理的血清IgA1失去了尾翼。 mirabilis 蛋白酶的作用很小，但是CH3结构域的丧失与结合Fcα受体的能力迅速丧失同时发生。用 P 处理过的S-IgA1。在相同条件下， mirabilis 蛋白酶保留了与Fcα受体结合的能力。结果与Fcα受体结合位点在CH2-CH3界面处一致。这些数据进一步阐明了S-IgA1的结构，并表明SC保护了S-IgA中Fcα受体的结合位点，从而延长了其在粘膜表面激活吞噬细胞的能力。

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