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首页> 外文期刊>Infection and immunity >Characterization of MspA, an Immunogenic Autotransporter Protein That Mediates Adhesion to Epithelial and Endothelial Cells in Neisseria meningitidis
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Characterization of MspA, an Immunogenic Autotransporter Protein That Mediates Adhesion to Epithelial and Endothelial Cells in Neisseria meningitidis

机译：MspA的表征，一种免疫原性自转运蛋白，介导对脑膜炎奈瑟氏球菌的上皮和内皮细胞粘附

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A novel putative autotransporter protein (NMB1998) was identified in the available genomic sequence of meningococcal strain MC58 (ET-5; ST-32). The mspA gene is absent from the genomic sequences of meningococcal strain Z2491 (ET-IV; ST-4) and the gonococcal strain FA1090. An orthologue is present in the meningococcal strain FAM18 (ET-37; ST-11), but the sequence contains a premature stop codon, suggesting that the protein may not be expressed in this strain. MspA is predicted to be a 157-kDa protein with low cysteine content, and it exhibits 36 and 33% identity to the meningococcal autotransporter proteins immunoglobulin A1 (IgA1) protease and App, respectively. Search of the Pfam database predicts the presence of IgA1 protease and autotransporter β-barrel domains. MspA was cloned, and a recombinant protein of the expected size was expressed and after being affinity purified was used to raise rabbit polyclonal monospecific antiserum. Immunoblot studies showed that ca. 125- and 95-kDa fragments of MspA are secreted in meningococcal strain MC58, which are absent from the isogenic mutant. Secretion of MspA was shown to be modified in an AspA isogenic mutant. A strain survey showed that MspA is expressed by all ST-32 and ST-41/44 (lineage 3) strains, but none of the ST-8 (A4) strains examined. Sera from patients convalescing from meningococcal disease were shown to contain MspA-specific antibodies. In bactericidal assays, anti-MspA serum was shown to kill the homologous strain (MC58) and another ST-32 strain. Escherichia coli-expressing recombinant MspA was shown to adhere to both human bronchial epithelial cells and brain microvascular endothelial cells.
机译：在脑膜炎球菌菌株MC58（ET-5; ST-32）的可用基因组序列中鉴定出一种新的推定的自转运蛋白（NMB1998）。脑膜炎球菌Z2491株（ET-IV; ST-4）和淋球菌FA1090的基因组序列中缺少 mspA 基因。直系同源物存在于脑膜炎球菌菌株FAM18（ET-37; ST-11）中，但该序列含有过早的终止密码子，表明该蛋白可能不在该菌株中表达。 MspA预计是一种低半胱氨酸含量的157 kDa蛋白，与脑膜炎球菌自转运蛋白免疫球蛋白A1（IgA1）蛋白酶和App分别具有36％和33％的同一性。 Pfam数据库的搜索预测了IgA1蛋白酶和自转运β-桶结构域的存在。克隆MspA，表达预期大小的重组蛋白，并在亲和纯化后用于产生兔多克隆单特异性抗血清。免疫印迹研究表明，大约MspA的125和95 kDa片段在脑膜炎球菌MC58株中分泌，而同基因突变体中却没有。在AspA等基因突变体中，MspA的分泌被修饰。菌株调查显示，MspA在所有ST-32和ST-41 / 44（谱系3）菌株中均表达，但没有检测到ST-8（A4）菌株。从脑膜炎球菌疾病中恢复的患者的血清显示含有MspA特异性抗体。在杀菌试验中，抗MspA血清被证明可以杀死同源菌株（MC58）和另一种ST-32菌株。表达大肠杆菌的重组MspA可以粘附在人支气管上皮细胞和脑微血管内皮细胞上。

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