Haag Nichole, Velk Kimberly, McCune Tyler, Wu Chun
The Natural Sciences Division, Mount Marty College, Yankton, SD 57078 USA.
Mount Marty College, Yankton, SD 57078 USA, She is now with Yankton High School.
World Acad Sci Eng Technol. 2015 Jun;9(6):587-591.
Methicillin/multiple-resistant (MRSA) are infectious bacteria that are resistant to common antibiotics. A previous 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 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.
耐甲氧西林/多重耐药(MRSA)是对常见抗生素具有抗性的传染性细菌。我们小组之前的一项研究已将假定蛋白SAV1226鉴定为潜在的药物靶点之一。在本研究中,我们报告了来自耐甲氧西林/万古霉素的Mu50菌株的假定蛋白SAV1226的生物信息学特征,以及克隆、表达、纯化和动力学分析。基质辅助激光解吸电离飞行时间质谱(MALDI-TOF/MS)分析显示与已知蛋白的结构相似性较低。动力学分析表明,假定蛋白SAV1226既不是ATP依赖性二羟基丙酮激酶的结构域,也不是磷酸转移酶系统(PTS)二羟基丙酮激酶的结构域,这表明假定蛋白SAV1226的功能可能在诸如UniProt和InterProScan 5等公共数据库中被错误注释。