Hiraga Noriyuki, Muratani Tetsuro, Naito Seiji, Matsumoto Tetsuro
Department of Urology, Graduate School of Medical Sciences, Kyushu University, Japan.
J Antibiot (Tokyo). 2008 Apr;61(4):213-21. doi: 10.1038/ja.2008.31.
We isolated faropenem-resistant Enterococcus faecalis in urine specimens and studied the mechanisms of resistance to faropenem in these isolates. Three mechanisms of penicillin resistance have been reported in E. faecalis; (1) beta-lactamase production, (2) overproduction of penicillin-binding protein (PBP) 4 or PBP5, and (3) decreasing affinities of penicillins for PBP4 by the occurrence of point mutations of the penicillin-binding domain. None of the E. faecalis isolates examined produced beta-lactamase or overproduced any PBPs, but the affinities of faropenem for PBP4 were decreased in faropenem-insensitive and -resistant strains. We found single amino acid substitutions at positions 475, 520 or 605 in PBP4 in the insensitive strains and two amino acid substitutions at positions 520 and 605 in PBP4 in the resistant strains by sequencing the entire pbp4 gene from each isolate. We conclude that development of resistance to faropenem in E. faecalis is due to decreasing affinities for PBP4 that are the result of the occurrence of one or two point mutations.
我们从尿液标本中分离出对法罗培南耐药的粪肠球菌,并研究了这些分离株对法罗培南的耐药机制。粪肠球菌中已报道了三种青霉素耐药机制:(1)产生β-内酰胺酶,(2)青霉素结合蛋白(PBP)4或PBP5过量产生,以及(3)青霉素结合结构域发生点突变导致青霉素对PBP4的亲和力降低。在所检测的粪肠球菌分离株中,没有一株产生β-内酰胺酶或过量产生任何PBP,但在对法罗培南不敏感和耐药的菌株中,法罗培南对PBP4的亲和力降低。通过对每个分离株的整个pbp4基因进行测序,我们在不敏感菌株的PBP4的475、520或605位发现了单个氨基酸取代,在耐药菌株的PBP4的520和605位发现了两个氨基酸取代。我们得出结论,粪肠球菌对法罗培南耐药性的产生是由于一个或两个点突变导致对PBP4的亲和力降低。