青霉素结合蛋白的重组表达及其在β-内酰胺类抗生素检测中的应用

Recombinant expression of penicillin binding proteins and application in detection of β-lactam antibiotics

中文关键词:  青霉素结合蛋白  重组表达  β-内酰胺类抗生素  免疫  检测

英文关键词:penicillin binding proteins  recombinant expression  β-lactam antibiotics  immunity  detection

中文摘要:

      目的 获得纯化的重组青霉素结合蛋白(penicillin binding proteins, PBPs), 研究其在β-内酰胺类抗生素检测中的应用。方法 以来源于肺炎链球菌Streptococcus pneumoniae R6的PBP2x蛋白为对照, 以PBP1a蛋白作为目标受体, 研究其与β-内酰胺类抗生素的亲和作用。结果 经纯化后的重组蛋白PBP2x和PBP1a检测头孢噻呋、青霉素G、氨苄青霉素、喷沙西林、阿莫西林的半抑制浓度(inhibitory concentration, IC50)都在7.02 ng/mL以下, 明确了PBP1a和PBP2x具有β-内酰胺类抗生素结合能力。结论 该研究为开发新的基于PBPs蛋白检测β-内酰胺类抗生素的免疫学方法奠定了基础。

英文摘要:

      Objective To obtain the purified recombinant penicillin binding proteins (PBPs) and study the application of these recombinant PBPs in the detection of β-lactam antibiotics. Methods The PBP2x protein derived from Streptococcus pneumoniae R6 was used as a control and PBP1a protein was used as the target receptor to study its affinity with β-lactam antibiotics. Results The purified recombinant proteins PBP2x and PBP1a detected for ceftiofur, penicillin G, ampicillin, pensacillin, and amoxicillin with inhibitory concentration (IC50) all below 7.02 ng/mL, which confirmed that PBP1a and PBP2x had β-lactam antibiotic binding ability. Conclusion This study lays the foundation for the development of a new immunological method based on PBPs protein to detect β-lactam antibiotics.