Controlling resistant bacteria with a novel class of β 2-lactamase inhibitor peptides: From rational design to in vivo analyses

Scientific Reports

Volumn 4, Issue , 2014, Pages

  Mandal, Santi M ^a   Migliolo, Ludovico ^b,c   Silva, Osmar N ^b   Fensterseifer, Isabel C M ^b   Faria Junior, Celio ^d   Dias, Simoni C ^b   Basak, Amit ^a   Hazra, Tapas K ^e   Franco, Octávio L ^b,c  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

^b Centro de Analises Proteomicas e Bioquymicas Pos Graduacao emCiencias Genomicas e Biotecnologia Universidade Catolica de Brasylia   (Brazil)

^c UNIVERSIDADE CATÓLICA DOM BOSCO   (Brazil)

^d Lacen Laboratório Central de Saúde Publica Do Distrito Federal   (Brazil)

^e University of Texas Medical Branch School of Medicine   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; PEPTIDE;

ANIMAL; ANTIBIOTIC RESISTANCE; BACILLUS CEREUS; BINDING SITE; CELL LINE; CELL SURVIVAL; CHEMISTRY; CYTOLOGY; DRUG DESIGN; DRUG EFFECTS; ENZYMOLOGY; ERYTHROCYTE; ESCHERICHIA COLI; KINETICS; METABOLISM; MICROBIAL SENSITIVITY TEST; MOLECULAR DOCKING; MOUSE; PROTEIN TERTIARY STRUCTURE; STAPHYLOCOCCUS AUREUS;

ANIMALS; ANTI-BACTERIAL AGENTS; BACILLUS CEREUS; BETA-LACTAMASE INHIBITORS; BETA-LACTAMASES; BINDING SITES; CELL LINE; CELL SURVIVAL; DRUG DESIGN; DRUG RESISTANCE, BACTERIAL; ERYTHROCYTES; ESCHERICHIA COLI; KINETICS; MICE; MICROBIAL SENSITIVITY TESTS; MOLECULAR DOCKING SIMULATION; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; STAPHYLOCOCCUS AUREUS;

EID: 84905912743     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep06015     Document Type: Article

References (36)

1. Levy, S. B. & Marshall, B. Antibacterial resistance worldwide: causes, challenges and responses. Nat. Med. 10, 122-129 (2004).
2. Sandora, T. J. & Goldmann, D. A. Preventing lethal hospital outbreaks of antibiotic-resistant bacteria. N Engl. J. Med. 367, 2168-70 (2012).
3. Turner, C. E. et al. Molecular analysis of an outbreak of lethal postpartum sepsis caused by Streptococcus pyogenes. J Clin Microbiol. 51, 2089-95 (2013).
4. Tse, H. et al. Molecular characterization of the 2011 Hong Kong scarlet fever outbreak. J. Infect Dis. 206, 341-51 (2012).
5. Walker, M. J. & Beatson, S. A. Epidemiology. Outsmarting outbreaks. Science 338, 1161-1162 (2012).
6. Sarraf-Yazdi, S. et al. A 9-Year retrospective review of antibiotic cycling in a surgical intensive care unit. J. Surg. Res. 176, e73-8 (2012).
7. Tenover, F. C. & Hughes, J. M. The challenges of emerging infectious diseases. Development and spread of multiply-resistant bacterial pathogens. JAMA 275, 300-304 (1996). (Pubitemid 26028589)
8. Jahnsen, R. D. et al. Antimicrobial activity of peptidomimetics against multidrugresistant Escherichia coli: a comparative study of different backbones. J. Med. Chem. 55, 7253-61 (2012).
9. Gary, W. et al. Binding properties of a peptide derived from lactamase inhibitory protein. Ant. Agents Chem. 45, 3279-3286 (2001).
10. Eidam, O. et al. Fragment-guided design of subnanomolar b-lactamase inhibitors active in vivo. Proc Natl Acad Sci USA. 109, 17448-53 (2012).
11. Rodkey, E. A. et al. Crystal structure of a preacylation complex of the b-lactamase inhibitor sulbactam bound to a sulfenamide bond-containing thiol-b-lactamase. J Am Chem Soc. 134, 16798-804 (2012).
12. Wang, S. H. et al. Thermodynamic analysis of the molecular interactions between amyloid beta-peptide 42 and (-)-epigallocatechin-3-gallate. J Phys Chem B. 114, 11576-11583 (2010).
13. Eidam, O. et al. Design, synthesis, crystal structures, and antimicrobial activity of sulfonamide boronic acids as beta-lactamase inhibitors. J Med Chem 53, 7852-7863 (2010).
14. Yuan, J. et al. Identification of a b-lactamase inhibitory protein variant that is a potent inhibitor of Staphylococcus PC1 b-lactamase. J Mol Biol. 406, 730-44 (2011).
15. Franco, O. L. Peptide promiscuity: an evolutionary concept for plant defense. FEBS Lett. 585, 995-1000 (2011).
16. Ripoll, A. In vitro selection of variants resistant to beta-lactams plus betalactamase inhibitors in CTX-M beta-lactamases: predicting the in vivo scenario? Antimicrob Agents Chemother. 55, 4530-4536 (2011).
17. Drawz, S. M. New b-lactamase inhibitors: a therapeutic renaissance in an "MDR world. Antimicrob Agents Chemother 58, 1835-46 (2014).
18. Tailford, L. E. et al.Mannose foraging by Bacteroides thetaiotaomicron: structure and specificity of the beta-mannosidase, BtMan2A. J Biol Chem 282, 11291-11299 (2007). (Pubitemid 47100757)
19. Wang, F. et al. Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature 471, 331-335 (2011).
20. Eswar, N. et al. [Comparative protein structure modeling using Modeller, Chapter 5]. [Curr Protoc Bioinformatics] [5-6] (John Wiley and Sons, London, 2006).
21. Sumathi, K. et al. 3dSS: 3D structural superposition. Nucleic Acids Res 34, W128-132 (2006). (Pubitemid 44529749)
22. Lano, D. The PyMOL molecular graphics system. DeLano Scientific, San Carlos, CA, USA 1 (2002).
23. Wilkins, M. R. et al. Protein identification and analysis tools in the ExPASy server. Methods Mol Biol 112, 531-552 (1999).
24. Stec, B. et al. Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme. Acta Crystallogr D Biol Crystallogr 61, 1072-1079 (2005). (Pubitemid 43951489)
25. Herzberg, O. Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution. J Mol Biol 217, 701-719 (1991). (Pubitemid 121003316)
26. Trott, O. & Olson, A. J. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31, 455-461 (2010).
27. Perez-Llarena, F. et al. The bla gene of the cephamycin cluster of Streptomyces clavuligerus encodes a class A beta-lactamase of low enzymatic activity. J Bacteriol 179, 6035-6040 (1997). (Pubitemid 27419026)
28. Institute, C. A. L. S. Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate. Methods for antimicrobial susceptibility testing of anaerobic bacteria; approved standard-eighth edition. CLSI document M11-A7. (2007).
29. O'Callaghan, C.H. et al.Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother 1, 283-288 (1972).
30. Lopez-Abarrategui, C. et al. Functional characterization of a synthetic hydrophilic antifungal peptide derived from the marine snail Cenchritis muricatus. Biochimie 94, 968-974 (2012).
31. Pasupuleti, M. et al. End-tagging of ultra-short antimicrobial peptides by W/F stretches to facilitate bacterial killing. PLoS One 4, e5285 (2009).
32. Laakkonen, P. et al. Antitumor activity of a homing peptide that targets tumor lymphatics and tumor cells. Proc Natl Acad Sci USA 101, 9381-9386 (2004). (Pubitemid 38812883)
33. Jasinski, M. et al. A novel mechanism of complement-independent clearance of red cells deficient in glycosyl phosphatidylinositol-linked proteins. Blood 103, 2827-2834 (2004). (Pubitemid 38393046)
34. Steinstraesser, L. et al. Innate defense regulator peptide 1018 in wound healing and wound infection. PloS One 7, e39373 (2012).
35. Jacobsen, F. et al. Activity of histone H1.2 in infected burn wounds. J Antimic Chem 55, 735-741 (2005). (Pubitemid 40691854)
36. Li, S. A., Lee, W. H. & Zhang, Y. Efficacy of OH-CATH30 and its analogs against drug-resistant bacteria in vitro and in mouse models. Antimicrob Agents Chemother 56, 3309-3317 (2012).