Structural characterization of an essential lipoprotein of Mycoplasma pneumoniae

Irem Keles, Sina Manger, Mbuso Siyabonga Mantanya, Achilleas S Frangakis
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Abstract

Mycoplasma pneumoniae is a human pathogen causing atypical community-acquired pneumonia. It is a model for a minimal cell, known for its non-canonical use of surface proteins for host-cell adhesion through ectodomain shedding and antigenic variation of surface proteins to evade the host cell immune response. Mpn444 is an essential mycoplasma surface protein implicated in both processes. It is one of 46 lipoproteins of M. pneumoniae, none of which have been structurally or functionally characterized. Here, we report the structure of Mpn444 at 3.04 Å as well as the molecular architecture of the trimeric Mpn444 complex. Our experimental structure displays striking similarity to structure predictions of several other essential lipoproteins in M. pneumoniae and other related Mycoplasma species, suggesting it to have a specialized and conserved function. The essentiality and involvement of Mpn444 in host immune evasion makes our structure a target for the development of new treatment strategies against mycoplasma infections.
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肺炎支原体必需脂蛋白的结构特征
肺炎支原体是一种导致非典型社区获得性肺炎的人类病原体。它是一种最小细胞模型,因其非典型使用表面蛋白通过外膜脱落粘附宿主细胞和表面蛋白抗原变异逃避宿主细胞免疫反应而闻名。Mpn444 是一种重要的支原体表面蛋白,与这两个过程都有关系。它是肺炎霉菌的 46 种脂蛋白之一,但没有一种脂蛋白具有结构或功能特征。在此,我们报告了 Mpn444 的 3.04 Å 结构以及 Mpn444 三聚体复合物的分子结构。我们的实验结构与肺炎双球菌和其他相关支原体中其他几种必需脂蛋白的结构预测显示出惊人的相似性,这表明它具有专门和保守的功能。Mpn444 在宿主免疫逃避中的重要性和参与性使我们的结构成为开发新的支原体感染治疗策略的目标。
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