Skip to main content
SpringerLink
Log in

The Metallo-β-Lactamases Fall into Two Distinct Phylogenetic Groups

  • Published:
Journal of Molecular Evolution Aims and scope Submit manuscript

Abstract

The Ambler Class B metallo-β-lactamases fall into two distinct phylogenetic groups based on the observation that there is no significant sequence homology between the sequences of members of different groups. Structural alignments confirm that those groups are no more closely related to each other than are the three classes of serine β-lactamases, Classes A, C, and D. We present phylogenies of these two groups and suggest a new classification scheme for the β-lactamases.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Figure 1
Figure 2

Similar content being viewed by others

References

  1. RP Ambler (1980) ArticleTitleThe structure of beta-lactamases. Philos Trans R Soc Lond B Biol Sci 289 321–331 Occurrence Handle6109327

    PubMed  Google Scholar 

  2. MB Avison CS Higgins CJ von Heldreich PM Bennett TR Walsh (2001) ArticleTitlePlasmid location and molecular heterogeneity of the L1 and L2 beta-lactamase genes of Stenotrophomonas maltophilia. Antimicrob Agents Chemother 45 413–419 Occurrence Handle10.1128/AAC.45.2.413-419.2001 Occurrence Handle11158734

    Article  PubMed  Google Scholar 

  3. M Barlow BG Hall (2002) ArticleTitlePhylogenetic analysis shows that the OXA β-lactamase genes have been on plasmids for millions of years. J Mol Evol 55 314–321 Occurrence Handle10.1007/s00239-002-2328-y Occurrence Handle12187384

    Article  PubMed  Google Scholar 

  4. S Bellais D Aubert T Naas P Nordmann (2000) ArticleTitleMolecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum. Antimicrob Agents Chemother 44 1878–1886 Occurrence Handle10.1128/AAC.44.7.1878-1886.2000 Occurrence Handle10858348

    Article  PubMed  Google Scholar 

  5. L Boschi PS Mercuri ML Riccio G Amicosante M Galleni JM Frere GM Rossolini (2000) ArticleTitleThe Legionella (Fluoribacter) gormanii metallo-beta-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 beta-lactamases. Antimicrob Agents Chemother 44 1538–1543 Occurrence Handle10.1128/AAC.44.6.1538-1543.2000 Occurrence Handle10817705

    Article  PubMed  Google Scholar 

  6. K Bush GA Jacoby AA Medeiros (1995) ArticleTitleA functional classification scheme for beta-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother 39 1211–1233 Occurrence Handle1:CAS:528:DyaK2MXlvFOntLo%3D Occurrence Handle7574506

    CAS  PubMed  Google Scholar 

  7. M Galleni J Lamotte-Brasseur GM Rossolini J Spencer O Dideberg JM Frere (2001) ArticleTitleStandard numbering scheme for class B beta-lactamases. Antimicrob Agents Chemother 45 660–663 Occurrence Handle10.1128/AAC.45.3.660-663.2001 Occurrence Handle11181339

    Article  PubMed  Google Scholar 

  8. BG Hall (2001) CodonAlign. Rochester NY

    Google Scholar 

  9. JP Huelsenbeck F Ronquist (2001) ArticleTitleMrBayes: Bayesian inference of phylogeny. Bioinformatics 17 754–755 Occurrence Handle10.1093/bioinformatics/17.8.754 Occurrence Handle1:STN:280:DC%2BD3MvotV2isw%3D%3D Occurrence Handle11524383

    Article  CAS  PubMed  Google Scholar 

  10. B Jaurin T Grundstrom (1981) ArticleTitleampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type. Proc Natl Acad Sci USA 78 4897–4901 Occurrence Handle6795623

    PubMed  Google Scholar 

  11. T Madej JF Gibrat SH Bryant (1995) ArticleTitleThreading a database of protein cores. Proteins 23 356–369 Occurrence Handle8710828

    PubMed  Google Scholar 

  12. M Ouellette L Bissonnette PH Roy (1987) ArticleTitlePrecise insertion of antibiotic resistance determinants into Tn21-like transposons: nucleotide sequence of the OXA-1 beta-lactamase gene. Proc Natl Acad Sci USA 84 7378–7382 Occurrence Handle2823258

    PubMed  Google Scholar 

  13. L Poirel T Naas D Nicolas L Collet S Bellais JD Cavallo P Nordmann (2000) ArticleTitleCharacterization of VIM-2, a carbapenem-hydrolyzing metallo-beta-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France. Antimicrob Agents Chemother 44 891–897 Occurrence Handle10.1128/AAC.44.4.891-897.2000 Occurrence Handle10722487

    Article  PubMed  Google Scholar 

  14. BA Rasmussen K Bush (1997) ArticleTitleCarbapenem-hydrolyzing beta-lactamases. Antimicrob Agents Chemother 41 223–232 Occurrence Handle9021171

    PubMed  Google Scholar 

  15. GM Rossolini T Walsh G Amicosante (1996) ArticleTitleThe Aeromonas metallo-beta-lactamases: Genetics, enzymology, and contribution to drug resistance. Microb Drug Resist 2 245–252 Occurrence Handle9158767

    PubMed  Google Scholar 

  16. GM Rossolini MA Condemi F Pantanella JD Docquier G Amicosante MC Thaller (2001) ArticleTitleMetallo-beta-lactamase producers in environmental microbiota: New molecular class B enzyme in Janthinobacterium lividum. Antimicrob Agents Chemother 45 837–844 Occurrence Handle10.1128/AAC.45.3.837-844.2001 Occurrence Handle11181369

    Article  PubMed  Google Scholar 

  17. TA Tatusova TL Madden (1999) ArticleTitleBLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol Lett 174 247–250 Occurrence Handle1:CAS:528:DyaK1MXjtlOlu74%3D Occurrence Handle10339815

    CAS  PubMed  Google Scholar 

  18. JD Thompson TJ Gibson F Plewniak F Jeanmougin DG Higgins (1997) ArticleTitleThe ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25 4876–4882 Occurrence Handle1:CAS:528:DyaK1cXntFyntQ%3D%3D Occurrence Handle9396791

    CAS  PubMed  Google Scholar 

  19. Z Wang W Fast AM Valentine SJ Benkovic (1999) ArticleTitleMetallo-beta-lactamase: structure and mechanism. Curr Opin Chem Biol 3 614–622 Occurrence Handle1:CAS:528:DyaK1MXmsleksLs%3D Occurrence Handle10508665

    CAS  PubMed  Google Scholar 

Download references

Acknowledgements

This study was supported by Grant GM60761 from the National Institutes of Health.

Author information

Authors and Affiliations

  1. Biology Department, Hutchison Hall, University of Rochester, Rochester, NY 14627-0211, USA

    Barry G. Hall, Stephen J. Salipante & Miriam Barlow

Authors
  1. Barry G. Hall
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Stephen J. Salipante
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Miriam Barlow
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Barry G. Hall.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hall, B.G., Salipante, S.J. & Barlow, M. The Metallo-β-Lactamases Fall into Two Distinct Phylogenetic Groups . J Mol Evol 57, 249–254 (2003). https://doi.org/10.1007/s00239-003-2471-0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00239-003-2471-0

Keywords

Search

Navigation