Bioinformatics and Molecular Biological Characterization of a Hypothetical Protein SAV1226 as a Potential Drug Target for Methicillin/Vancomycin-Staphylococcus aureus Infections.

Nichole Haag, Kimberly Velk, Tyler McCune, Chun Wu
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Abstract

Methicillin/multiple-resistant Staphylococcus aureus (MRSA) are infectious bacteria that are resistant to common antibiotics. A previous in silico study in our group has identified a hypothetical protein SAV1226 as one of the potential drug targets. In this study, we reported the bioinformatics characterization, as well as cloning, expression, purification and kinetic assays of hypothetical protein SAV1226 from methicillin/vancomycin-resistant Staphylococcus aureus Mu50 strain. MALDI-TOF/MS analysis revealed a low degree of structural similarity with known proteins. Kinetic assays demonstrated that hypothetical protein SAV1226 is neither a domain of an ATP dependent dihydroxyacetone kinase nor of a phosphotransferase system (PTS) dihydroxyacetone kinase, suggesting that the function of hypothetical protein SAV1226 might be misannotated on public databases such as UniProt and InterProScan 5.

假设蛋白SAV1226作为甲氧西林/万古霉素-金黄色葡萄球菌感染的潜在药物靶点的生物信息学和分子生物学特性
甲氧西林/多重耐药金黄色葡萄球菌(MRSA)是对常见抗生素耐药的感染性细菌。我们小组先前的一项计算机研究已经确定了一种假设的蛋白质SAV1226作为潜在的药物靶点之一。在本研究中,我们报道了耐甲氧西林/万古霉素金黄色葡萄球菌Mu50菌株中假设蛋白SAV1226的生物信息学特征、克隆、表达、纯化和动力学分析。MALDI-TOF/MS分析显示其与已知蛋白的结构相似性较低。动力学分析表明,假设的蛋白SAV1226既不是ATP依赖性二羟丙酮激酶的结构域,也不是磷酸转移酶系统(PTS)二羟丙酮激酶的结构域,这表明假设的蛋白SAV1226的功能可能在UniProt和InterProScan 5等公共数据库中被错误注释。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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