این سایت در حال حاضر پشتیبانی نمی شود و امکان دارد داده های نشریات بروز نباشند
Iranian Biomedical Journal، جلد ۲۵، شماره ۳، صفحات ۱۹۳-۲۰۱
عنوان فارسی
چکیده فارسی مقاله
کلیدواژه‌های فارسی مقاله
عنوان انگلیسی Stereochemical Trajectories of a Two-Component Regulatory System PmrA/B in a Colistin-Resistant Acinetobacter baumannii Clinical Isolate
چکیده انگلیسی مقاله Background: There is limited information on the three-dimensional (3D) prediction and modeling of the colistin resistance-associated proteins PmrA/B TCS in Acinetobacter baumannii. We aimed to evaluate the stereochemical structure and domain characterization of phosphotransferase membrane receptor A/B (PmrA/B) in an A. baumannii isolate resistant to high-level colistin, using bioinformatics tools. Methods: The species of the isolate and its susceptibility to colistin were confirmed by PCR-sequencing and minimum inhibitory concentration assay, respectively. For 3D prediction of the PmrA/B, we used 16 template models with the highest quality (e-value <1 × 10−50). Results: Prediction of the PmrA structure revealed a monomeric non-redundant protein consisting of 28 α-helices and 22 β-sheets. The PmrA DNA-binding motif displayed three antiparallel α-helices, followed by three β-sheets, and was bond to the major groove of DNA by intermolecular van der Waals bonds through amino acids Lys, Asp, His, and Arg, respectively. Superimposition of the deduced PmrA 3D structure with the closely related PmrA protein model (GenBank no. WP_071210493.1) revealed no distortion in conformation, due to Glu→Lys substitution at position 218. Similarly, the PmrB protein structure displayed 24 α-helices and 13 β-sheets. In our case, His251 acted as a phosphate receptor in the HisKA domain. The amino acid substitutions were mainly observed at the putative N-terminus region of the protein. Furthermore, two substitutions (Lys21→Ser and Ser28→Arg) in the transmembrane domain were detected. Conclusion: The DNA-binding motif of PmrA is highly conserved, though the N-terminal fragment of PmrB showed a high rate of base substitutions. This research provides valuable insights into the mechanism of colistin resistance in A. baumannii.
کلیدواژه‌های انگلیسی مقاله Acinetobacter baumannii, Amino acid substitution, Colistin, Mutation
نویسندگان مقاله | Mohammad Reza Kandehkar-Ghahraman
Department of Microbiology and Virology, Kerman University of Medical Sciences, Kerman, Iran


| Hossein Hosseini-Nave
Department of Microbiology and Virology, Kerman University of Medical Sciences, Kerman, Iran


| Omid Azizi
Department of Laboratory Sciences, School of Paramedical Sciences, Torbat Heydariyeh University of Medical sciences, Torbat Heydariyeh, Iran


| Mohammad Reza Shakibaie
Department of Microbiology and Virology, Kerman University of Medical Sciences, Kerman, Iran


| Hamid Mollaie
Research Center for Tropical and Infectious Diseases Kerman University of Medical Sciences, Kerman, Iran


| Samane Shakibaie
Student Research Committee, Kerman University of Medical Sciences, Kerman, Iran
نشانی اینترنتی http://ibj.pasteur.ac.ir/browse.php?a_code=A-10-4269-1&slc_lang=en&sid=1
فایل مقاله فایلی برای مقاله ذخیره نشده است
کد مقاله (doi)
زبان مقاله منتشر شده en
موضوعات مقاله منتشر شده Molecular Microbiology
نوع مقاله منتشر شده مقاله کامل
برگشت به: صفحه اول پایگاه   |   نسخه مرتبط   |   نشریه مرتبط   |   فهرست نشریات