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首页> 外文期刊>Infection and immunity >A Naturally Occurring Single-Residue Mutation in the Translocator Domain of Neisseria meningitidis NhhA Affects Trimerization, Surface Localization, and Adhesive Capabilities
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A Naturally Occurring Single-Residue Mutation in the Translocator Domain of Neisseria meningitidis NhhA Affects Trimerization, Surface Localization, and Adhesive Capabilities

机译：脑膜炎奈瑟氏球菌NhhA易位域中自然发生的单残基突变影响三聚化，表面定位和粘附能力。

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Neisseria meningitidis NhhA (Neisseria hia/hsf homologue A) is an oligomeric outer membrane protein belonging to the family of trimeric autotransporter adhesins. NhhA mediates the interaction of N. meningitidis with human epithelial cells and components of the extracellular matrix. The recombinant protein is able to induce bactericidal antibodies and hence has also been considered a potential vaccine candidate. In this study, we analyzed the production of NhhA in a large panel of N. meningitidis strains belonging to different serogroups and clonal complexes. We found that trimeric NhhA was produced at different levels by the various strains tested. In some strains belonging to the clonal complex ST41/44, the protein is detectable only as a monomer. Sequencing of the nhhA gene and generation of complementing strains in different genetic backgrounds have proved that a single mutation (Gly to Asp) in the translocator domain affected both trimerization and surface localization of NhhA. In vitro infection assays showed that this mutation impairs meningococcal NhhA-mediated adhesion, suggesting that strains carrying the mutation may rely on different strategies or molecules to mediate interaction with host cells. Finally, we demonstrated that N. meningitidis ST41/44 strains producing the mutated form did not induce killing mediated by NhhA-specific bactericidal antibodies. Our data help to elucidate the secretion mechanisms of trimeric autotransporters and to understand the contribution of NhhA in the evolutionary process of host-Neisseria interactions. Also, they might have important implications for the evaluation of NhhA as a vaccine candidate.
机译：脑膜炎奈瑟氏球菌NhhA（Neisseria hia / hsf同源物A）是一种寡聚外膜蛋白，属于三聚体自转运粘附素家族。 NhhA介导脑膜炎奈瑟氏球菌与人上皮细胞和细胞外基质成分的相互作用。重组蛋白能够诱导杀菌抗体，因此也被认为是潜在的疫苗候选物。在这项研究中，我们分析了一大批属于不同血清群和克隆复合体的脑膜炎奈瑟氏球菌菌株中NhhA的产生。我们发现三聚NhhA是由各种测试菌株以不同水平产生的。在属于克隆复合物ST41 / 44的某些菌株中，仅作为单体可以检测到该蛋白质。 nhhA 基因的测序和在不同遗传背景下互补菌株的产生已证明，易位域中的单个突变（从Gly到Asp）影响NhhA的三聚化和表面定位。 体外感染试验表明，该突变削弱了脑膜炎球菌NhhA介导的粘附，表明携带该突变的菌株可能依赖于不同的策略或分子来介导与宿主细胞的相互作用。最后，我们证明产生突变形式的脑膜炎奈瑟氏球菌ST41 / 44菌株不诱导由NhhA特异性杀菌抗体介导的杀伤。我们的数据有助于阐明三聚体自转运蛋白的分泌机制，并了解NhhA在宿主-奈瑟氏菌相互作用的进化过程中的贡献。同样，它们可能对评估NhhA作为候选疫苗具有重要意义。

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