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首页> 外文期刊>Acta crystallographica. Section D, Structural biology >Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins
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Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins

机译：SdgB——SdgA-mediated结构依据葡萄球菌胶蛋白质的糖基化

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摘要

The initiation of infection of host tissues by Staphylococcus aureus requires a family of staphylococcal adhesive proteins containing serine-aspartate repeat (SDR) domains, such as ClfA. The O-linked glycosylation of the long-chain SDR domain mediated by SdgB and SdgA is a key virulence factor that protects the adhesive SDR proteins against host proteolytic attack in order to promote successful tissue colonization, and has also been implicated in staphylococcal agglutination, which leads to sepsis and an immunodominant epitope for a strong antibody response. Despite the biological significance of these two glycosyltransferases involved in pathogenicity and avoidance of the host innate immune response, their structures and the molecular basis of their activity have not been investigated. This study reports the crystal structures of SdgB and SdgA from S. aureus as well as multiple structures of SdgB in complex with its substrates (for example UDP, N-acetylglucosamine or SDR peptides), products (glycosylated SDR peptides) or phosphate ions. Together with biophysical and biochemical analyses, this structural work uncovered the novel mechanism by which SdgB and SdgA carry out the glycosyl-transfer process to the long SDR region in SDR proteins. SdgB undergoes dynamic changes in its structure such as a transition from an open to a closed conformation upon ligand binding and takes diverse forms, both as a homodimer and as a heterodimer with SdgA. Overall, these findings not only elucidate the putative role of the three domains of SdgB in recognizing donor and acceptor substrates, but also provide new mechanistic insights into glycosylation of the SDR domain, which can serve as a starting point for the development of antibacterial drugs against staphylococcal infections.
机译：感染的宿主组织的起始金黄色葡萄球菌需要一个家庭葡萄球菌胶蛋白含serine-aspartate重复(SDR)领域,如ClfA。长链特别提款权域由SdgB和SdgA是一个重要的毒力因子,保护了吗胶特别提款权对宿主蛋白水解蛋白质攻击为了促进成功的组织殖民,也被卷入葡萄球菌的凝集,从而导致脓毒症和immunodominant抗原决定基的强抗体反应。这两种糖基转移酶的重要性参与的致病性和避免宿主先天免疫反应,他们的结构和他们的活动没有的分子基础被调查。SdgB结构和SdgA金黄色葡萄球菌以及多个SdgB结构复杂以其底物(例如UDP,N-acetylglucosamine或特别提款权肽),产品(糖基化的特别提款权肽)或磷酸离子。与生物物理和生物化学分析,揭示了这种结构性工作小说SdgB和SdgA执行机制glycosyl-transfer过程漫长的特别提款权地区特别提款权蛋白质。它的结构变化,如过渡从开放到封闭的构象配体作为一个绑定,以多样化的形式为作为一个与SdgA异质二聚体。总的来说,这些发现不仅阐明了假定的SdgB的三个领域的作用识别供体和受体底物,但是还提供新机械的见解糖基化的特别提款权域,可以作为发展的起点抗菌药物对葡萄球菌感染。

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