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,IC_(50))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。
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(IC_(50))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.
作者
刘艳容
黄璐
李宁
顾慧丹
周帆
胡飞杰
杨瑶
LIU Yan-Rong;HUANG Lu;LI Ning;GU Hui-Dan;ZHOU Fan;HU Fei-Jie;YANG Yao(Nanjing Institute of Product Quality Inspection,Nanjing 210019,China;School of Tourism and Culinary Arts,Zhejiang Business College,Hangzhou 310053,China;School of Food Science and Pharmaceutical Engineering,Nanjing Normal University,Nanjing 210023,China)
出处
《食品安全质量检测学报》
CAS
北大核心
2022年第1期156-162,共7页
Journal of Food Safety and Quality
基金
南京市市场监督管理局重点科技项目(Kj2019001)
国家市场监督管理总局科技计划项目(2020MK136、2020MK139)。
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
penicillin binding proteins
recombinant expression
β-lactam antibiotics
immunity
detection
