Mohamed Sofia B, Adlan Talal A, Khalafalla Nagla A, Abdalla Nusiba I, Ali Zainab Sa, Munir Ka Abdella, Hassan Mohamed M, Elnour Mohammed-Ahmed B
Department of Bioinformatics and Biostatistics, National University Biomedical Research Institute, National University, Khartoum-Sudan.
Faculty of Medicine, National University, Khartoum, Sudan.
Evol Bioinform Online. 2019 Jul 16;15:1176934319864945. doi: 10.1177/1176934319864945. eCollection 2019.
Whole genome sequencing of methicillin-resistant (MRSA) strain isolated from Sudan has led to a great deal of information, which allows the identification and characterization of some pivotal proteins. The objective of this study was to investigate the penicillin-binding proteins, PBP and PBP2a, of SO-1977 strain to have insights about their physicochemical properties and to assess and describe the interaction of some phytochemicals against them in silico. PBP and PBP2a from MRSA's Sudan strain were found to be of great resemblance with some other strains. G246E single-nucleotide polymorphism was reported and identified in the allosteric binding site positioned in the non-penicillin-binding domain. The docked compounds demonstrated good binding energies and hydrogen bond interactions with residue Ser404 which plays crucial roles in β-lactam activity. This finding would contribute significantly to designing effective β-lactam drugs, to combat and treat β-lactam-resistant bacteria in the future.
对从苏丹分离出的耐甲氧西林金黄色葡萄球菌（MRSA）菌株进行全基因组测序，已获得大量信息，这些信息有助于鉴定和表征一些关键蛋白。本研究的目的是研究SO-1977菌株的青霉素结合蛋白（PBP）和PBP2a，以深入了解它们的物理化学性质，并在计算机模拟中评估和描述一些植物化学物质与它们的相互作用。发现来自MRSA苏丹菌株的PBP和PBP2a与其他一些菌株非常相似。在位于非青霉素结合域的变构结合位点中报告并鉴定了G246E单核苷酸多态性。对接的化合物表现出良好的结合能，并与在β-内酰胺活性中起关键作用的Ser404残基形成氢键相互作用。这一发现将为未来设计有效的β-内酰胺药物以对抗和治疗耐β-内酰胺细菌做出重大贡献。
