Effects of altering aminoglycoside structures on bacterial resistance enzyme activities

Antimicrobial Agents and Chemotherapy

Volumn 55, Issue 7, 2011, Pages 3207-3213

  Green, Keith D ^c   Chen, Wenjing ^b,c   Garneau Tsodikova, Sylvie ^a,b,c  

^a Department of Medicinal Chemistry ^*  (United States)

^b Chemical Biology Doctoral Program   (United States)

^c Life Sciences Institute   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIKACIN; AMINOGLYCOSIDE; AMINOGLYCOSIDE ACETYLTRANSFERASE; AMINOGLYCOSIDE MODIFYING ENZYME; BACTERIAL ENZYME; GENTAMICIN; KANAMYCIN A; NEOMYCIN; PAROMOMYCIN; RIBOSTAMYCIN; SISOMICIN; TOBRAMYCIN; UNCLASSIFIED DRUG;

ACETYLATION; AMINO ACID SEQUENCE; ANTIBACTERIAL ACTIVITY; ARTICLE; BACILLUS SUBTILIS; DRUG STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; IN VIVO STUDY; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL;

AMINOGLYCOSIDES; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; CHROMATOGRAPHY, THIN LAYER; GENTAMICINS; MASS SPECTROMETRY; MICROBIAL SENSITIVITY TESTS;

EID: 79959277696     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00312-11     Document Type: Article

References (33)

1. Azucena, E., I. Grapsas, and S. Mobashery. 1997. Properties of a bifunctional bacterial antibiotic resistance enzyme that catalyzes ATP-dependent 2″-phosphorylation and acetyl-CoA-dependent 6′-acetylation of aminoglycosides. J. Am. Chem. Soc. 119:2317-2318.
2. Boehr, D. D., D. M. Daigle, and G. D. Wright. 2004. Domain-domain interactions in the aminoglycoside antibiotic resistance enzyme AAC(6′)- APH(2″). Biochemistry 43:9846-9855.
3. Borovinskaya, M. A., et al. 2007. Structural basis for aminoglycoside inhibition of bacterial ribosome recycling. Nat. Struct. Mol. Biol. 14:727-732.
4. Burk, D. L., N. Ghuman, L. E. Wybenga-Groot, and A. M. Berghuis. 2003. X-ray structure of the AAC(6′)-Ii antibiotic resistance enzyme at 1.8 Å resolution; examination of oligomeric arrangements in GNAT superfamily members. Protein Sci. 12:426-437.
5. Burk, D. L., W. C. Hon, A. K. Leung, and A. M. Berghuis. 2001. Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase. Biochemistry 40:8756-8764.
6. Carter, A. P., et al. 2000. Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature 407:340-348.
7. Centrón, D., and P. H. Roy. 2002. Presence of a group II intron in a multiresistant Serratia marcescens strain that harbors three integrons and a novel gene fusion. Antimicrob. Agents Chemother. 46:1402-1409.
8. Daigle, D. M., D. W. Hughes, and G. D. Wright. 1999. Prodigious substrate specificity of AAC(6′)-APH(2″), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci. Chem. Biol. 6:99-110.
9. GES-1 and a fused product of aac(3)-Ib/aac(6[dprime])-Ib″ gene cassettes in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 46:638-645.
10. Fong, D. H., and A. M. Berghuis. 2009. Structural basis of APH(3′)-IIIa-mediated resistance to N1-substituted aminoglycoside antibiotics. Antimicrob. Agents Chemother. 53:3049-3055.
11. Fong, D. H., and A. M. Berghuis. 2002. Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry. EMBO J. 21:2323-2331.
12. Green, K. D., W. Chen, J. L. Houghton, M. Fridman, and S. Garneau-Tsodikova. 2010. Exploring the substrate promiscuity of drug-modifying enzymes for the chemoenzymatic generation of N-acylated aminoglycosides. Chembiochem 11:119-126.
13. Houghton, J. L., K. D. Green, W. Chen, and S. Garneau-Tsodikova. 2010. The future of aminoglycosides: the end or renaissance? Chembiochem 11:880-902.
14. Kim, C., D. Hesek, J. Zajicek, S. B. Vakulenko, and S. Mobashery. 2006. Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3″)-Ii/AAC(6′)-IId from Serratia marcescens. Biochemistry 45:8368-8377. (Pubitemid 44036543)
15. Kim, C., A. Villegas-Estrada, D. Hesek, and S. Mobashery. 2007. Mechanistic characterization of the bifunctional aminoglycoside-modifying enzyme AAC(3)-Ib/AAC(6′)-Ib′ from Pseudomonas aeruginosa. Biochemistry 46:5270-5282. (Pubitemid 46683023)
16. Magalhães, M. L., and J. S. Blanchard. 2005. The kinetic mechanism of AAC3-IV aminoglycoside acetyltransferase from Escherichia coli. Biochemistry 44:16275-16283.
17. Magalhães, M. L., et al. 2008. Kinetic and structural analysis of bisubstrate inhibition of the Salmonella enterica aminoglycoside 6′-N-acetyltransferase. Biochemistry 47:579-584. (Pubitemid 351195429)
18. Maurice, F., et al. 2008. Enzyme structural plasticity and the emergence of broad-spectrum antibiotic resistance. EMBO Rep. 9:344-349.
19. Nurizzo, D., et al. 2003. The crystal structure of aminoglycoside- 3′-phosphotransferase- IIa, an enzyme responsible for antibiotic resistance. J. Mol. Biol. 327:491-506.
20. Pedersen, L. C., M. M. Benning, and H. M. Holden. 1995. Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry 34:13305-13311.
21. Porter, V. R., K. D. Green, O. E. Zolova, J. L. Houghton, and S. Garneau-Tsodikova. 2010. Dissecting the cosubstrate structure requirements of the Staphylococcus aureus aminoglycoside resistance enzyme ANT(4′). Biochem. Biophys. Res. Commun. 403:85-90.
22. Shaul, P., et al. 2011. Assessment of 6′- and 6″-N-acylation of aminoglycosides as a strategy to overcome bacterial resistance. Org. Biomol. Chem. 9:4057-4063.
23. Stogios, P. J., T. Shakya, E. Evdokimova, A. Savchenko, and G. D. Wright. 2011. Structure and function of APH(4)-Ia, a hygromycin B resistance enzyme. J. Biol. Chem. 286:1966-1975.
24. Thompson, P. R., D. W. Hughes, and G. D. Wright. 1996. Regiospecificity of aminoglycoside phosphotransferase from enterococci and staphylococci (APH(3′)-IIIa). Biochemistry 35:8686-8695.
25. Toth, M., J. W. Chow, S. Mobashery, and S. B. Vakulenko. 2009. Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2″-phosphotransferases. J. Biol. Chem. 284:6690-6696.
26. Toth, M., H. Frase, N. T. Antunes, C. A. Smith, and S. B. Vakulenko. 2010. Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase-2″-IVa. Protein Sci. 19:1565-1576.
27. Vetting, M. W., S. S. Hegde, F. Javid-Majd, J. S. Blanchard, and S. L. Roderick. 2002. Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nat. Struct. Biol. 9:653-658.
28. Vetting, M. W., S. Magnet, E. Nieves, S. L. Roderick, and J. S. Blanchard. 2004. A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones. Chem. Biol. 11:565-573.
29. Vetting, M. W., et al. 2008. Mechanistic and structural analysis of aminoglycoside N-acetyltransferase AAC(6′)-Ib and its bifunctional, fluoroquinoloneactive AAC(6′)-Ib-cr variant. Biochemistry 47:9825-9835.
30. Wolf, E., et al. 1998. Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase. Cell 94:439-449. (Pubitemid 28391860)
31. Wybenga-Groot, L. E., K. Draker, G. D. Wright, and A. M. Berghuis. 1999. Crystal structure of an aminoglycoside 6′-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold. Structure 7:497-507.
32. Young, P. G., et al. 2009. The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside-2″- phosphotransferase- IIa [APH(2″)-IIa] provide insights into substrate selectivity in the APH(2″) subfamily. J. Bacteriol. 191:4133-4143.
33. Zhang, W., J. F. Fisher, and S. Mobashery. 2009. The bifunctional enzymes of antibiotic resistance. Curr. Opin. Microbiol. 12:505-511.