PDF(Pubmed)
Abstract：
S-layers are crystalline arrays found on bacterial and archaeal cells. Lactobacillus is a diverse family of bacteria known especially for potential gut health benefits. This study focuses on the S-layer proteins from Lactobacillus acidophilus and Lactobacillus amylovorus common in the mammalian gut. Atomic resolution structures of Lactobacillus S-layer proteins SlpA and SlpX exhibit domain swapping, and the obtained assembly model of the main S-layer protein SlpA aligns well with prior electron microscopy and mutagenesis data. The S-layer\'s pore size suggests a protective role, with charged areas aiding adhesion. A highly similar domain organization and interaction network are observed across the Lactobacillus genus. Interaction studies revealed conserved binding areas specific for attachment to teichoic acids. The structure of the SlpA S-layer and the suggested incorporation of SlpX as well as its interaction with teichoic acids lay the foundation for deciphering its role in immune responses and for developing effective treatments for a variety of infectious and bacteria-mediated inflammation processes, opening opportunities for targeted engineering of the S-layer or lactobacilli bacteria in general.
摘要：
S层是在细菌和古细菌细胞上发现的晶体阵列。乳杆菌是一种多样化的细菌家族，尤其以潜在的肠道健康益处而闻名。这项研究的重点是哺乳动物肠道中常见的嗜酸乳杆菌和淀粉乳杆菌的S层蛋白。乳杆菌S层蛋白SlpA和SlpX的原子分辨率结构表现出结构域交换，并且所获得的主要S层蛋白SlpA的组装模型与先前的电子显微镜和诱变数据良好地对齐。S层的孔径表明了保护作用，带电区域帮助粘附。在乳杆菌属中观察到高度相似的域组织和相互作用网络。相互作用研究揭示了与磷壁酸结合的保守结合区。SlpAS层的结构和建议的SlpX的掺入及其与磷壁酸的相互作用为破译其在免疫反应中的作用以及开发各种感染性和细菌介导的炎症过程的有效治疗奠定了基础。为一般的S层或乳杆菌细菌的靶向工程开辟了机会。
