Murakami K, Fujimura T, Doi M
Kanzakigawa Laboratory, Shionogi and Co., Ltd., Osaka, Japan.
FEMS Microbiol Lett. 1994 Apr 1;117(2):131-6. doi: 10.1111/j.1574-6968.1994.tb06754.x.
The structural gene for penicillin-binding protein 2 (PBP2) of Staphylococcus aureus was cloned and sequenced. The nucleotide sequence of the 2,458-bp chromosomal fragment was determined, and the 2,148-bp coding region for PBP2 was identified. Determination of ten N-terminal amino acids of the PBP2 protein indicated that N-terminal methionine had been removed from the primary translational product. Thus, PBP2 is comprised of 715 amino acids with a molecular mass of 79,147. Nucleotide sequences having some homology with the PBP2 gene and proteins cross-reactive with anti-PBP2 antibody were detected in some other species of staphylococci by polymerase chain reaction and Western blot analysis, respectively.
克隆并测定了金黄色葡萄球菌青霉素结合蛋白2（PBP2）的结构基因。确定了2458bp染色体片段的核苷酸序列，并鉴定出PBP2的2148bp编码区。对PBP2蛋白的十个N端氨基酸进行测定表明，初级翻译产物中的N端甲硫氨酸已被去除。因此，PBP2由715个氨基酸组成，分子量为79147。分别通过聚合酶链反应和蛋白质印迹分析在其他一些葡萄球菌物种中检测到了与PBP2基因具有一定同源性的核苷酸序列以及与抗PBP2抗体发生交叉反应的蛋白质。
