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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Chang, Tein-Yao Huang, Bo-Jun Sun, Jun-Ren Perng, Cherng-Lih Chan, Ming-Chin Yu, Cheng-Ping Chiueh, Tzong-Shi |
| Description | Author Affiliation: Chang TY ( Graduate Institute of Medical Sciences, National Defense Medical Center, Taipei, Taiwan); Huang BJ ( Division of Clinical Pathology, Department of Pathology, Tri-Service General Hospital, National Defense Medical Center, Taipei, Taiwan); Sun JR ( Graduate Institute of Medical Sciences, National Defense Medical Center, Taipei, Taiwan); Perng CL ( Division of Clinical Pathology, Department of Pathology, Tri-Service General Hospital, National Defense Medical Center, Taipei, Taiwan.); Chan MC ( Infection Control Office, Tri-Service General Hospital, Taipei, Taiwan.); Yu CP ( Institute of Preventive Medicine, National Defense Medical Center, Taipei, Taiwan.); Chiueh TS ( Division of Clinical Pathology, Department of Pathology, Tri-Service General Hospital, National Defense Medical Center, Taipei, Taiwan) |
| Abstract | Overexpression of the efflux pump AdeABC is associated with tigecycline resistance of multi-drug resistant Acinetobacter baumannii (MDRAB). A two-component regulatory system, sensor AdeS and regulator AdeR proteins regulate the pump. However, the detailed mechanism of the AdeR protein to enhance the expression of adeABC operon is not well defined. We illustrated the biological characteristics of AdeR proteins by comparing a mutant AdeR protein of a tigecycline resistant MDRAB to the wild AdeR protein. By analyzing a series of deletion constructs, a minimal gene cassette of the intercistronic spacer DNA fragment specifically bound with the adeR protein and resulted in band shifting in electrophoresis mobility shifting assays (EMSA). A conserve direct repeat motif was observed in the intercistronic spacer DNA. We demonstrated the AdeR protein was a direct-repeat-binding protein. Two common residue mutations on the AdeR proteins of tigecycline resistant MDRAB isolates could reduce their binding affinity with the intercistronic spacer. The free intercistronic spacer may then more efficiently support the read-through of the adeABC operon during the co-transcriptional translation in tigecycline resistant MDRAB isolates. |
| File Format | HTM / HTML |
| ISSN | 09445013 |
| Journal | Microbiological Research |
| Volume Number | 183 |
| e-ISSN | 16180623 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-02-01 |
| Publisher Place | Germany |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Microbiology Discipline Environmental Health |
| Content Type | Text |
| Resource Type | Article |
| Subject | Microbiology |
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