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首页> 外文期刊>BMC Microbiology >The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins
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The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins

机译：肺炎链球菌的高度保守的丝氨酸苏氨酸激酶StkP有助于青霉素的敏感性，独立于编码青霉素结合蛋白的基因

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Background The serine/threonine kinase StkP of Streptococcus pneumoniae is a major virulence factor in the mouse model of infection. StkP is a modular protein with a N-terminal kinase domain a C-terminal PASTA domain carrying the signature of penicillin-binding protein (PBP) and prokaryotic serine threonine kinase. In laboratory cultures, one target of StkP is the phosphoglucosamine mutase GlmM involved in the first steps of peptidoglycan biosynthesis. In order to further elucidate the importance of StkP in S. pneumoniae, its role in resistance to β-lactams has been assessed by mutational analysis in laboratory cultures and its genetic conservation has been investigated in isolates from infected sites (virulent), asymptomatic carriers, susceptible and non-susceptible to β-lactams. Results Deletion replacement mutation in stkP conferred hypersensitivity to penicillin G and was epistatic on mutations in PBP2X, PBP2B and PBP1A from the resistant 9V clinical isolate URA1258. Genetic analysis of 55 clinical isolates identified 11 StkP alleles differing from the reference R6 allele. None relevant mutation in the kinase or the PASTA domains were found to account for susceptibility of the isolates. Rather the minimal inhibitory concentration (MIC) values of the strains appeared to be determined by their PBP alleles. Conclusion The results of genetic dissection analysis in lab strain Cp1015 reveal that StkP is involved in the bacterial response to penicillin and is epistatic on mutations PBP 2B, 2X and 1A. However analysis of the clinical isolates did not allow us to find the StkP alleles putatively involved in determining the virulence or the resistance level of a given strain, suggesting a strong conservation of StkP in clinical isolates.
机译：背景肺炎链球菌的丝氨酸/苏氨酸激酶StkP是小鼠感染模型中的主要毒力因子。 StkP是具有N末端激酶结构域和C末端PASTA结构域的模块化蛋白，带有青霉素结合蛋白（PBP）和原核丝氨酸苏氨酸激酶的签名。在实验室培养中，StkP的一个靶标是参与肽聚糖生物合成第一步的磷酸葡糖胺突变酶GlmM。为了进一步阐明StkP在肺炎链球菌中的重要性，已通过实验室培养中的突变分析评估了其对β-内酰胺的抗性作用，并已从感染部位（无毒），无症状携带者，对β-内酰胺敏感和不敏感。结果stkP中的缺失替换突变赋予了对青霉素G的超敏性，并且对耐药9V临床分离株URA1258的PBP2X，PBP2B和PBP1A突变具有上位性。对55个临床分离株的遗传分析确定了11个与参考R6等位基因不同的StkP等位基因。没有发现激酶或PASTA结构域中的相关突变解释了分离物的敏感性。相反，菌株的最小抑菌浓度（MIC）值似乎由其PBP等位基因决定。结论实验室菌株Cp1015的遗传解剖分析结果表明StkP参与了细菌对青霉素的反应，并且在PBP 2B，2X和1A突变上具有上位性。但是，对临床分离株的分析不能使我们找到推定参与确定给定菌株的毒力或耐药水平的StkP等位基因，这表明StkP在临床分离株中具有很强的保守性。

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