Evidence map›Paper›PMID 27332861›Full record

ArticlePLoS computational biology2016

Novel Computational Protocols for Functionally Classifying and Characterising Serine Beta-Lactamases.

David Lee, Sayoni Das, Natalie L Dawson, Dragana Dobrijevic, John Ward, Christine Orengo

Abstract read
In one paragraph

Article in PLoS computational biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Defense mechanisms ofFrontiers in antibiotics · 2024
    Review
  4. Article
  5. β-lactam Resistance inPathogens (Basel, Switzerland) · 2021
    Review
  6. Article
  7. Computational intelligence and neuroscience · 2021
    Article
  8. Article
  9. Emerging Strategies to Combat β-Lactamase Producing ESKAPE Pathogens.International journal of molecular sciences · 2020
    Review
  10. Review
  11. Past and Present Perspectives on β-Lactamases.Antimicrobial agents and chemotherapy · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

David LeeInstitute of Structural and Molecular Biology, University College London, London, United Kingdom.ORCID 0000-0003-1794-2232
Sayoni DasInstitute of Structural and Molecular Biology, University College London, London, United Kingdom.
Natalie L DawsonInstitute of Structural and Molecular Biology, University College London, London, United Kingdom.
Dragana DobrijevicDepartment of Biochemical Engineering, University College London, London, United Kingdom.
John WardDepartment of Biochemical Engineering, University College London, London, United Kingdom.ORCID 0000-0002-4415-5544
Christine OrengoInstitute of Structural and Molecular Biology, University College London, London, United Kingdom.

Funding

Wellcome Trust
6 · The paper itself

Abstract

Beta-lactamases represent the main bacterial mechanism of resistance to beta-lactam antibiotics and are a significant challenge to modern medicine. We have developed an automated classification and analysis protocol that exploits structure- and sequence-based approaches and which allows us to propose a grouping of serine beta-lactamases that more consistently captures and rationalizes the existing three classification schemes: Classes, (A, C and D, which vary in their implementation of the mechanism of action); Types (that largely reflect evolutionary distance measured by sequence similarity); and Variant groups (which largely correspond with the Bush-Jacoby clinical groups). Our analysis platform exploits a suite of in-house and public tools to identify Functional Determinants (FDs), i.e. residue sites, responsible for conferring different phenotypes between different classes, different types and different variants. We focused on Class A beta-lactamases, the most highly populated and clinically relevant class, to identify FDs implicated in the distinct phenotypes associated with different Class A Types and Variants. We show that our FunFHMMer method can separate the known beta-lactamase classes and identify those positions likely to be responsible for the different implementations of the mechanism of action in these enzymes. Two novel algorithms, ASSP and SSPA, allow detection of FD sites likely to contribute to the broadening of the substrate profiles. Using our approaches, we recognise 151 Class A types in UniProt. Finally, we used our beta-lactamase FunFams and ASSP profiles to detect 4 novel Class A types in microbiome samples. Our platforms have been validated by literature studies, in silico analysis and some targeted experimental verification. Although developed for the serine beta-lactamases they could be used to classify and analyse any diverse protein superfamily where sub-families have diverged over both long and short evolutionary timescales.

Indexed as

AlgorithmsSoftwarebeta-Lactamase Inhibitorsbeta-Lactamasesbeta-Lactam ResistanceBinding SitesComputer SimulationDrug Resistance, BacterialEnzyme ActivationMolecular Docking SimulationProtein BindingSequence Analysis, ProteinSerineStructure-Activity RelationshipSubstrate Specificitybeta-Lactamase Inhibitorsbeta-LactamasesSerine

Identifiers

PMID27332861
PMCPMC4917113

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.