Ploscariu Nicoleta T, Herrera Alvaro I, Jayanthi Srinivas, Suresh Kumar Thallapuranam K, Geisbrecht Brian V, Prakash Om
Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS, 66506, USA.
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, 72701, USA.
Biomol NMR Assign. 2017 Oct;11(2):285-288. doi: 10.1007/s12104-017-9764-5. Epub 2017 Aug 16.
The bacterium Staphylococcus aureus produces an array of anti-inflammatory molecules that prevent the innate immune system from recognizing it as a pathogen and clearing it from the host. In the acute phase of inflammation, our immune system relies on neutrophils to clear invading bacteria. Recently, novel classes of secreted proteins from S. aureus, including the Extracellular Adherence Protein (EAP) family (Stapels et al., Proc Natl Acad Sci USA 111:13187-13192, 2014) and the Staphylococcal Peroxidase Inhibitor (SPIN), (unpublished work) have been identified as highly selective inhibitors acting on Neutrophil Serine Proteases (NSPs) and myeloperoxidase (MPO) respectively. SPIN is a protein found only in Staphylococci, with no sequence homology to any known proteins. Solution NMR structural studies of SPIN are therefore expected to provide a deeper understanding of its interaction with MPO. In this study, we report the backbone and side-chain H, N, and C resonance assignments of SPIN. Furthermore, using the chemical shifts of these resonances, we predicted the secondary structure of SPIN in solution via the TALOS-N server. The assignment data has been deposited in the BMRB data bank under Accession No. 27069.
金黄色葡萄球菌会产生一系列抗炎分子，这些分子可阻止先天免疫系统将其识别为病原体并将其从宿主体内清除。在炎症的急性期，我们的免疫系统依靠中性粒细胞来清除入侵的细菌。最近，已鉴定出金黄色葡萄球菌分泌的新型蛋白质类别，包括细胞外粘附蛋白（EAP）家族（Stapels等人，《美国国家科学院院刊》111:13187 - 13192，2014年）和葡萄球菌过氧化物酶抑制剂（SPIN）（未发表的研究），它们分别是作用于中性粒细胞丝氨酸蛋白酶（NSPs）和髓过氧化物酶（MPO）的高选择性抑制剂。SPIN是一种仅在葡萄球菌中发现的蛋白质，与任何已知蛋白质均无序列同源性。因此，对SPIN进行溶液核磁共振结构研究有望更深入地了解其与MPO的相互作用。在本研究中，我们报告了SPIN的主链和侧链的H、N和C共振归属。此外，利用这些共振的化学位移，我们通过TALOS - N服务器预测了SPIN在溶液中的二级结构。该归属数据已存入BMRB数据库，登录号为27069。
