School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei, 230009, China.
Arch Microbiol. 2021 Jul;203(5):2563-2573. doi: 10.1007/s00203-021-02255-0. Epub 2021 Mar 8.
Heparin, known for its anticoagulant activity, is commonly used as the coatings of medical devices. The attaching of Staphylococcus aureus, a prominent human and animal pathogen, to the heparin coatings usually leads to catheter-related bloodstream infections. Hence, the study of the interaction between heparin and S. aureus surface proteins is desired. Here, we found that protein A (SpA) of S. aureus was a heparin-binding protein, contributing to the interaction between S. aureus and heparin. The cell-wall-anchored SpA was one of the most critical S. aureus virulence factors with a lysin-like motif (LysM). When SpA was mutated to remove the LysM motif, the heparin-binding capability of SpA dropped 50%. The in-frame deletion of spa also reduced the heparin-binding capability of S. aureus. There was 1.3-fold more of heparin bound to wild type S. aureus than the Δspa::Em strain. These results would help understand the host-microbe interaction and the infection by S. aureus.
肝素由于其抗凝活性而被广泛应用于医疗器械的涂层。金黄色葡萄球菌（一种重要的人和动物病原体）附着在肝素涂层上通常会导致导管相关的血流感染。因此，研究肝素与金黄色葡萄球菌表面蛋白之间的相互作用是很有必要的。在这里，我们发现金黄色葡萄球菌的蛋白 A（SpA）是一种肝素结合蛋白，有助于金黄色葡萄球菌与肝素之间的相互作用。锚定在细胞壁上的 SpA 是金黄色葡萄球菌最重要的毒力因子之一，具有溶菌酶样结构域（LysM）。当 SpA 发生突变去除 LysM 结构域时，SpA 的肝素结合能力下降了 50%。spa 的框内缺失也降低了金黄色葡萄球菌的肝素结合能力。与Δspa::Em 菌株相比，野生型金黄色葡萄球菌结合的肝素多了 1.3 倍。这些结果有助于我们理解宿主-微生物的相互作用以及金黄色葡萄球菌的感染机制。
