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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lu, Jun Jiang, Shan Li, Chao-Pin Li, Ying Liu, Qian-Ying Ma, Shuai |
| Description | Author Affiliation: Lu J ( Department of Pathogen Biology and Immunology, Anhui University of Science and Technology, Huainan, Anhui 232001, P.R. China.); Jiang S ( Department of Mining Engineering, Huainan Vocational and Technical College, Huainan, Anhui 232001, P.R. China.); Liu QY ( Department of Pathogen Biology and Immunology, Anhui University of Science and Technology, Huainan, Anhui 232001, P.R. China.); Ma S ( Department of Pathogen Biology and Immunology, Anhui University of Science and Technology, Huainan, Anhui 232001, P.R. China.); Li Y ( Department of Pathogen Biology and Immunology, Anhui University of Science and Technology, Huainan, Anhui 232001, P.R. China.); Li CP ( Department of Medical Parasitology, Wannan Medical College, Wuhu, Anhui 241002, P.R. China.) |
| Abstract | The aim of the present study was to investigate the mutational characteristics of drugresistant genetic mutations in the katG gene to isoniazid (INH) in multidrug resistant Mycobacterium tuberculosis (MTB) Lform among patients with pneumoconiosis complicated with tuberculosis (TB), in order to reduce the occurrence of drug resistance in patients, and gain further insight into the mechanisms underlying drug resistance in MDRTB Lform. A total of 114 clinically isolated strains of MTB Lforms were collected. The MDRTB Lforms were identified using a conventional antimicrobial susceptibility test (AST). The DNA genomes were extracted, the target genes were amplified by polymerase chain reaction technology and the hotspot mutational regions in the katG gene were analyzed by direct sequencing. The results of AST analysis demonstrated that there were 31 strains of MDRTB Lforms in 114 clinical isolates. The mutation rate of katG was 61.29% (19/31) in INHresistant isolates, mainly concentrated in codon 315 (Ser315Thr, 48.39% and Ser315Asn, 9.68%) and 431 (Ala431Val, 3.23%). Base substitutions were identified, however, no multisite mutations were found. No mutations in katG were identified in 10 INHsensitive strains that were randomly selected. INHresistance was more severe in MDRTB Lform isolates among patients with pneumoconiosis complicated with TB. The substitution of highly conserved amino acids encoded by the katG gene resulted in the molecular mechanisms responsible for INH resistance in MDRTB Lform isolates. It was also verified that the katG gene was in diversiform. The katG Ser315Thr mutation is one of the main causes of resistance to INH in MDRTB L-form isolates. |
| ISSN | 17912997 |
| e-ISSN | 17913004 |
| Journal | Molecular Medicine Reports |
| Issue Number | 5 |
| Volume Number | 9 |
| Language | English |
| Publisher | Spandidos Publications |
| Publisher Date | 2014-05-01 |
| Publisher Place | Greece |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Genetics Catalase Mutation Mycobacterium Tuberculosis Pneumoconiosis Complications Tuberculosis, Multidrug-resistant Microbiology Antitubercular Agents Pharmacology Dna Mutational Analysis Microbial Sensitivity Tests Drug Effects Sequence Analysis, Dna Research Support, Non-u.s. Gov't Discipline Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Biochemistry Molecular Biology Cancer Research Molecular Medicine Oncology |
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