Evaluation of gidB alterations responsible for streptomycin resistance in Mycobacterium tuberculosis

Journal of Antimicrobial Chemotherapy

Volumn 69, Issue 11, 2014, Pages 2935-2941

  Verma, Jitender S ^a   Gupta, Yash ^b   Nair, Deepthi ^a   Manzoor, Nikhat ^c   Rautela, Rajinder S ^d   Rai, Arvind ^d   Katoch, Vishwa M ^e  

^a SAFDARJUNG HOSPITAL   (India)

^b NATIONAL JALMA INSTITUTE FOR LEPROSY AND OTHER MYCOBACTERIAL DISEASES   (India)

^c JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

^d National Centre for Disease Control   (India)

^e GOVERNMENT OF INDIA   (India)

Author keywords

DNA sequencing; Drug resistance; In silico modelling; Novel mutations

Indexed keywords

BACTERIAL PROTEIN; GIDB PROTEIN; STREPTOMYCIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT;

AMINO ACID SUBSTITUTION; ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; BACTERIAL STRAIN; BACTERIUM ISOLATE; CODON; COMPUTER MODEL; ENZYME ACTIVE SITE; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PHENOTYPE; POINT MUTATION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; CHEMISTRY; CLINICAL TRIAL; DRUG EFFECTS; EVALUATION STUDY; GENETICS; HUMAN; MICROBIAL SENSITIVITY TEST; MULTICENTER STUDY; MUTATION; PROCEDURES;

ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; DRUG RESISTANCE, BACTERIAL; HUMANS; MICROBIAL SENSITIVITY TESTS; MUTATION; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, SECONDARY; STREPTOMYCIN;

EID: 84923865353     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dku273     Document Type: Article

References (31)

1. WHO. Global Tuberculosis Report 2013. Geneva, Switzerland: WHO, 2013.
2. Harris WH, William N, Stuart MG. In: Tuberculosis. Boston: Little Brown, 1996; 745-61.
3. Ruiz P, Rodríguez-Cano F, Zerolo FJ et al. Investigation of the in vitro activity of streptomycin against Mycobacterium tuberculosis. Microbial Drug Resist 2002; 8:147-9.
4. Fourmy D, Recht MI, Puglisi JD. Binding of neomycin-class aminoglycoside antibiotics to the A-site of 16 S rRNA. J Mol Biol 1998; 277:347-62.
5. Magnet S, Blanchard JS. Molecular insights into aminoglycoside action and resistance. Chemother Rev 2005; 105:477-98.
6. Melancon P, Lemieux C, Brakier-Gingras L. A mutation in the 530 loop of Escherichia coli 16S ribosomal RNA causes resistance to streptomycin. Nucleic Acids Res 1988; 16:9631-9.
7. Finken M, Krischner P, Meier A et al. Molecular basis of streptomycin resistance in Mycobacterium tuberculosis: alterations of the ribosomal protein S12 gene and point mutations within a functional 16S ribosomal RNA pseudoknot. Mol Microbiol 1993; 9:1239-46.
8. Sreevatsan S, Pan X, Stockbauer KE et al. Characterization of rpsL and rrs mutations in streptomycin-resistant Mycobacterium tuberculosis isolates from diverse geographic localities. Antimicrob Agents Chemother 1996; 40:1024-6.
9. Okamoto S, Tamaru A, Nakajima C et al. Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria. Mol Microbiol 2007; 63, 1096-106.
10. Melancon P, Tapprich WE, Brakier-Gingras L. Single-base mutations at position 2661 of Escherichia coli 23S rRNA increase efficiency of translational proofreading. J Bacteriol 1992; 174:7896-901.
11. Powers T, Noller HF. A functional pseudoknot in 16S ribosomal RNA. EMBO J 1991; 10:2203-14.
12. Springer B, Kidan YG, Prammananan Tet al. Mechanisms of streptomycin resistance: selection of mutations in the 16S rRNA gene conferring resistance. Antimicrob Agents Chemother 2001; 45:2877-84.
13. Ogle JM, Ramakrishnan V. Structural insights into translational fidelity. Annu Rev Biochem 2005; 74:129-77.
14. Perdigão J, Macedo R, Machado D et al. GidB mutation as a phylogenetic marker for Q1 cluster Mycobacterium tuberculosis isolates and intermediate-level streptomycin resistance determinant in Lisbon, Portugal. Clin Microbiol Infect 2014; 20: O278-84.
15. Romanowski MJ, Bonanno JB, Burley SK. Crystal structure of the Escherichia coli glucose-inhibited division protein B (GidB) reveals a methyltransferase fold. Proteins 2002; 47:563-7.
16. Srivastava K, Das R, Sharma VD et al. Relevance of degree of rifampicin resistance in M. tuberculosis. Ind J Med Microbiol 2001; 19:36-9.
17. Bastian I, Colebunders R. Treatment and prevention of multidrugresistant tuberculosis. Drugs 1999; 58:633-61.
18. Wong SY, Lee JS, Kwak HK et al. Mutations in gidB confer low-level streptomycin resistance in Mycobacterium tuberculosis. Antimicrob Agents Chemother 2011; 55:2515-22.
19. Fernanda SS, Pedro E, Almeida DS et al. Identification of mutations related to streptomycin resistance in clinical isolates of Mycobacterium tuberculosis and possible involvement of efflux mechanism. Antimicrob Agents Chemother 2008; 8:2947-9.
20. Roy A, Kucukural A, Zhang Y. I-TASSER: a unified platformfor automated protein structure and function prediction. Nat Protoc 2010; 5:725-38.
21. Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graph 1996; 14:33-8.
22. Schneidman-Duhovny D, Inbar Y, Nussinov R et al. Geometry-based flexible and symmetric protein docking. Proteins 2005; 60:224-31.
23. Andrusier N, Nussinov R, Wolfson HJ. FireDock: fast interaction refinement in molecular docking. Proteins 2007; 69:139-59.
24. Mashiach E, Schneidman-Duhovny D, Andrusier N et al. FireDock: aweb server for fast interaction refinement in molecular docking. Nucleic Acids Res 2008; 36:229-32.
25. Cooksey RC, Morlock GP, McQueen A et al. Characterization of streptomycin resistance patients in New York City. Antimicrob Agents Chemother 1996; 40:1186-8.
26. Douthwaite S, Fourmy D, Yoshizawa S. Nucleotide methylations in rRNA that confer resistance to ribosome-targeting antibiotics. In: Grosjean H, ed. Fine-Tuning of RNA Functions by Modification and Editing. New York: Springer, 2005; 287-309.
27. Poehlsgaard P, Douthwaite S. The bacterial ribosome as a target for antibiotics. Nat Rev Microbiol 2005; 3:870-81.
28. Perdigao J, Sabino A, Milho C et al. Characterization of gidB gene in Mycobacterium tuberculosis isolates in Lisbon Health Region: role in streptomycin resistance and epidemiological markers. In: Abstracts of the Thirtieth Annual Congress of the European Society ofMycobacteriology, Porto, Portugal, 2009. Abstract PP-41, p. 113. European Society of Mycobacteriology.
29. Siddiqi N, Shamim M, Hussain S et al. Molecular characterization of multidrug-resistant isolates of Mycobacterium tuberculosis from patients in North India. Antimicrob Agents Chemother 2002; 46:443-50.
30. Honore N, Marchal G, Cole ST. Novel mutation in 16S rRNA associated with streptomycin dependence in Mycobacterium tuberculosis. Antimicrob Agents Chemother 1995; 39:769-70.
31. Meier A, Sander P, Schaper KJ et al. Correlation of molecular resistance mechanisms and phenotypic resistance levels in streptomycin-resistant Mycobacterium tuberculosis. Antimicrob Agents Chemother 1996; 40:2452-4.