Gehrlein M, Leying H, Cullmann W, Wendt S, Opferkuch W
Abteilung Medizinische Mikrobiologie und Immunologie, Ruhr-Universität Bochum, BRD.
Chemotherapy. 1991;37(6):405-12. doi: 10.1159/000238887.
The comparison of a clinical Acinetobacter baumanii isolate (strain No. 4852/88) and its selected imipenem-resistant (IMR) clone exhibited a complex reorganization of the penicillin-binding proteins (PBPs) with diminished labelling of all PBPs except the 24-kD PBP which showed an increased binding of 14C-penicillin. This protein could not be saturated by preincubation of membranes with imipenem at 8-fold the MIC of imipenem, thus indicating PBP alterations responsible for imipenem resistance. In A. baumanii 4852/88 seven PBPs with the apparent molecular weights of 94, 84, 65, 61, 48, 40 and 24 kD could be detected. beta-Lactamase production was barely detectable in any case and could not be enhanced in the presence of various beta-lactams as the inducer. The outer membrane proteins were found identical in both the wild-type strain and the Im clone. So far, imipenem-resistant A. baumanii isolates have been isolated twice in our diagnostic laboratory; however, no implications on the future relevance of the above findings can be made.
一株临床鲍曼不动杆菌分离株（菌株编号4852/88）与其筛选出的亚胺培南耐药（IMR）克隆株的比较显示，青霉素结合蛋白（PBPs）发生了复杂的重组，除24-kD的PBP外，所有PBPs的标记减少，而该24-kD的PBP显示14C-青霉素结合增加。用亚胺培南MIC的8倍浓度预孵育膜不能使该蛋白饱和，因此表明PBP改变是亚胺培南耐药的原因。在鲍曼不动杆菌4852/88中可检测到7种表观分子量分别为94、84、65、61、48、40和24 kD的PBPs。在任何情况下几乎检测不到β-内酰胺酶的产生，并且在各种β-内酰胺作为诱导剂存在的情况下也不能增强。野生型菌株和IM克隆株的外膜蛋白相同。到目前为止，我们诊断实验室已两次分离出亚胺培南耐药的鲍曼不动杆菌分离株；然而，对于上述发现未来的相关性无法得出结论。
