| Literature DB >> 31786767 |
Waleska Yana Lazaretti1, Elaine Luzia Dos Santos1, José Luis da-Conceição Silva1, Marina Kimiko Kadowaki1, Rinaldo Ferreira Gandra2, Alexandre Maller1, Rita de Cássia Garcia Simão3.
Abstract
The role of the clpB gene encoding HSP/chaperone ClpB was evaluated in the multiresistant antibiotic cells of Acinetobacter baumannii (RS4 strain) under stress-induced heat shock and different beta-lactams. The expression of the clpB gene was assessed by qPCR during heat shock at 45 °C and subinhibitory concentrations of ampicillin (30 μg mL-1), amoxicillin + sulbactam (8/12 μg mL-1), cefepime (30 μg mL-1), sulfamethoxazole + trimethoprim (120/8 μg mL-1) and meropenem (18 μg mL-1). The results indicated a transient increase in clpB transcription in all treatments except cefepime. Both in the presence of ampicillin and amoxicillin/sulbactam for 20 min, the mRNA-clpB synthesis was 1.4 times higher than that of the control at time zero. Surprisingly, the mRNA-clpB levels were more than 30-fold higher after 10 min of incubation with meropenem and more than eightfold higher in the presence of trimethoprim/sulfamethoxazole. In addition, western blot assays showed that the RS4 strain treated with meropenem showed a marked increase in ClpB protein expression. Our data indicate that during exposure to beta-lactams, A. baumannii adjusts the transcription levels of the clpB mRNA and protein to respond to stress, suggesting that the chaperone may act as a key cellular component in the presence of antibiotics in this bacterium.Entities:
Keywords: Antibiotics; ClpB; Heat shock proteins; Multidrug resistance; Stress response
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Year: 2019 PMID: 31786767 DOI: 10.1007/s11033-019-05209-4
Source DB: PubMed Journal: Mol Biol Rep ISSN: 0301-4851 Impact factor: 2.316