Protein & Cell >

2020 , Vol. 11 >Issue 8: 613 - 617

DOI: https://doi.org/10.1007/s13238-020-00736-4

LETTER

Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse

  • Marcelo Monteiro Pedroso 1,2 ,
  • David W. Waite 1,2 ,
  • Okke Melse 3 ,
  • Liam Wilson 1 ,
  • Nataša Mitić 4 ,
  • Ross P. McGeary 1 ,
  • Iris Antes 3 ,
  • Luke W. Guddat 1 ,
  • Philip Hugenholtz , 1,2 ,
  • Gerhard Schenk , 1,2
Expand
  • 1. School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, QLD, Brisbane 4072, Australia
  • 2. Australian Centre for Ecogenomics, The University of Queensland, St. Lucia, QLD, Brisbane 4072, Australia
  • 3. Center for Integrated Protein Science Munich at the TUM School of Life Sciences, Technische Universität München, 85354 Freising, Germany
  • 4. Department of Chemistry, Maynooth University, Maynooth, Co. Kildare, Ireland

Published date: 15 Aug 2020

Copyright

2020 The Author(s)
Fold

Cite this article

Marcelo Monteiro Pedroso , David W. Waite , Okke Melse , Liam Wilson , Nataša Mitić , Ross P. McGeary , Iris Antes , Luke W. Guddat , Philip Hugenholtz , Gerhard Schenk . Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse[J]. Protein & Cell, 2020 , 11(8) : 613 -617 . DOI: 10.1007/s13238-020-00736-4

References

Publishing order | Descend order by publishing year | Descend order by cited within
1
Bush K, Jacoby GA (2010) Updated functional classification of β- lactamases. Antimicrob Agents Chemther 54(3):969–976

DOI

2
Drawz SM, Bethel CR, Doppalapudi VR, Sheri A, Pagadala SR, Hujer AM, Skalweit MJ, Anderson VE, Chen SG, Buynak JD (2010) Penicillin sulfone inhibitors of class D β-lactamases. Antimicrob Agents Chemother 54(4):1414–1424

DOI

3
Khan AU, Maryam L, Zarrilli R (2017) Structure, genetics and worldwide Spread of New Delhi metallo-β-lactamase (NDM): a threat to public health. BMC Microbiol 17(1):101

DOI

4
Laxminarayan R, Duse A, Wattal C, Zaidi AK, Wertheim HF, Sumpradit N, Vlieghe E, Hara GL, Gould IM, Goossens H (2013) Antibiotic resistance—the need for global solutions. Lancet Infect Dis 13(12):1057–1098

DOI

5
Lee JH, Takahashi M, Jeon JH, Kang LW, Seki M, Park KS, Hong MK, Park YS, Kim TY, Karim AM (2019) Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo- β-lactamases: a molecular and evolutionary study. Emerg Microbes Infect 8:1688–1700

DOI

6
Lisa MN, Palacios AR, Aitha M, González MM, Moreno DM, Crowder MW, Bonomo RA, Spencer J, Tierney DL, Llarrull LI (2017) A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases. Nat Commun 8(1):538

DOI

7
McGeary RP, Tan DT, Schenk G (2017) Progress toward inhibitors of metallo-β-lactamases. Future Med Chem 9(7):673–691

DOI

8
Mitic N, Miraula M, Selleck C, Hadler KS, Uribe E, Pedroso MM, Schenk G (2014) Catalytic mechanisms of metallohydrolases containing two metal ions. Adv Protein Chem Struct Biol 97:49–81

DOI

9
Moran-Barrio J, Lisa MN, Larrieux N, Drusin SI, Viale AM, Moreno DM, Buschiazzo A, Vila AJ (2016) Crystal structure of the metallo-β-lactamase GOB in the periplasmic dizinc form reveals an unusual metal site. Antimicrob Agents Chemother 60 (10):6013–6022

DOI

10
Parks DH, Chuvochina M, Waite DW, Rinke C, Skarshewski A, Chaumeil PA, Hugenholtz P (2018) A standardized bacterial taxonomy based on genome phylogeny substantially revises the tree of life. Nat Biotechnol 36(10):996–1004

DOI

11
Selleck CL, Larrabee J, Harmer J, Guddat LW, Mitić N, Helweh W, Ollis DL, Craig WA, Tierney DL, Pedroso MM, Schenk G (2016) AIM-1: an antibiotic-degrading metallohydrolase that displays mechanistic flexibility. Chem Eur J 22(49):17704–17714

DOI

12
Sun Z, Mehta SC, Adamski CJ, Gibbs RA, Palzkill T (2016) Deep sequencing of random mutant libraries reveals the active site of the narrow specificity CphA metallo-β-lactamase is fragile to mutations. Nat Sci Rep 6:33195

DOI

13
Vella P, Miraula M, Phelan E, Leung EW, Ely F, Ollis DL, McGeary RP, Schenk G, Mitic N (2013) Identification and characterization of an unusual metallo-β-lactamase from Serratia proteamacu- lans. J Biol Inorg Chem 18(7):855–863

DOI

14
Walsh TR, Toleman MA, Poirel L, Nordmann P (2005) Metallo-β- lactamases: the quiet before the storm? Clin Microbiol Rev 18 (2):306–325

DOI

15
Yong D, Toleman MA, Bell J, Ritchie B, Pratt R, Ryley H, Walsh TR (2012) Genetic and biochemical characterization of an acquired subgroup B3 metallo-β-lactamase gene, blaAIM-1, and its unique genetic context in Pseudomonas aeruginosa from Australia. Antimicrob Agents Chemother 56(12):6154

DOI

Options
Outlines

/

〈 〉