Antibiotic resistance in Zn(II)-deficient environments: Metallo-β-lactamase activation in the periplasm

Future Microbiology

Volumn 8, Issue 8, 2013, Pages 947-949

  Meini, María Rocío ^a   González, Lisandro J ^a   Vila, Alejandro J ^a  

^a UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

Author keywords

antibiotic resistance; metallo lactamases; nutritional immunity; periplasm; Zn(II)

Indexed keywords

BETA LACTAM ANTIBIOTIC; CALGRANULIN; CARBAPENEM DERIVATIVE; CEPHALOSPORIN DERIVATIVE; IMIPENEM; LACTAM; MANGANESE; METALLO BETA LACTAMASE; ZINC ION;

ACINETOBACTER BAUMANNII; ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; BACTERIAL GROWTH; CYTOPLASM; DOWN REGULATION; ENZYME ACTIVATION; ESCHERICHIA COLI; IN VITRO STUDY; IN VIVO STUDY; MULTIDRUG RESISTANCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PSEUDOMONAS AERUGINOSA; REVIEW;

BACTERIA; BETA-LACTAM RESISTANCE; BETA-LACTAMS; COENZYMES; PERIPLASM; PROTEIN BINDING; ZINC;

EID: 84881291707     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.13.34     Document Type: Review

References (20)

1. Andreini C, Bertini I, Rosato A. Metalloproteomes: A bioinformatic approach. Acc. Chem. Res. 42 (10), 1471-1479 (2009).
2. Ma Z, Jacobsen FE, Giedroc DP. Coordination chemistry of bacterial metal transport and sensing. Chem. Rev. 109 (10), 4644-4681 (2009).
3. Outten CE, O'Halloran TV. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292 (5526), 2488-2492 (2001).
4. Hood MI, Skaar EP. Nutritional immunity: Transition metals at the pathogen-host interface. Nat. Rev. Microbiol. 10 (8), 525-537 (2012).
5. Kehl-Fie TE, Skaar EP. Nutritional immunity beyond iron: A role for manganese and zinc. Curr. Opin. Chem. Biol. 14 (2), 218-224 (2010).
6. Brophy MB, Hayden JA, Nolan EM. Calcium ion gradients modulate the zinc affinity and antibacterial activity of human calprotectin. J. Am. Chem. Soc. 134 (43), 18089-18100 (2012).
7. Hood MI, Mortensen BL, Moore JL et al. Identification of an Acinetobacter baumannii zinc acquisition system that facilitates resistance to calprotectin-mediated zinc sequestration. PLoS Pathog. 8 (12), e1003068 (2012).
8. Dieppois G, Ducret V, Caille O, Perron K. The transcriptional regulator CzcR modulates antibiotic resistance and quorum sensing in Pseudomonas aeruginosa. PLoS ONE 7 (5), e38148 (2012).
9. Walsh TR, Toleman MA, Poirel L, Nordmann P. Metallo-beta-lactamases: The quiet before the storm? J. Am. Chem. Soc. 18 (2), 306-325 (2005).
10. Crowder MW, Spencer J, Vila AJ. Metallo-beta-lactamases: Novel weaponry for antibiotic resistance in bacteria. Acc. Chem. Res. 39 (10), 721-728 (2006).
11. Galleni M, Lamotte-Brasseur J, Rossolini GM, Spencer J, Dideberg O, Frere JM. Standard numbering scheme for class B beta-lactamases. Antimicrob. Agents Chemother. 45 (3), 660-663 (2001).
12. King DT, Worrall LJ, Gruninger R, Strynadka NC. New Delhi metallo-beta-lactamase: Structural insights into beta-lactam recognition and inhibition. J. Am. Chem. Soc. 134 (28), 11362-11365 (2012).
13. Tioni MF, Llarrull LI, Poeylaut-Palena AA et al. Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase. J. Am. Chem. Soc. 130 (47), 15852-15863 (2008).
14. Wommer S, Rival S, Heinz U et al. Substrate-activated zinc binding of metallo-beta-lactamases: Physiological importance of mononuclear enzymes. J. Biol. Chem. 277 (27), 24142-24147 (2002).
15. Moran-Barrio J, Limansky AS, Viale AM. Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: Completion of folding and Zn (II) ion acquisition occur in the bacterial periplasm. Antimicrob. Agents Chemother. 53 (7), 2908-2917 (2009).
16. Hu Z, Gunasekera TS, Spadafora L, Bennett B, Crowder MW. Metal content of metallo-beta-lactamase L1 is determined by the bioavailability of metal ions. Biochemistry 47 (30), 7947-7953 (2008).
17. Moran-Barrio J, Gonzalez JM, Lisa MN et al. The metallo-beta-lactamase GOB is a mono-Zn (II) enzyme with a novel active site. J. Biol. Chem. 282 (25), 18286-18293 (2007).
18. Harris WR, Keen C. Calculations of the distribution of zinc in a computer model of human serum. J. Nutr. 119 (11), 1677-1682 (1989).
19. Berducci G, Mazzetti AP, Rotilio G, Battistoni A. Periplasmic competition for zinc uptake between the metallochaperone ZnuA and Cu,Zn superoxide dismutase. FEBS Lett. 569 (1-3), 289-292 (2004).
20. Gonzalez JM, Meini MR, Tomatis PE, Medrano Martin FJ, Cricco JA, Vila AJ. Metallo-beta-lactamases withstand low Zn (II) conditions by tuning metal-ligand interactions. Nat. Chem. Biol. 8 (8), 698-700 (2012).