Evidence map›Paper›PMID 35205122›Full record

ArticleBiology2022

New CTX-M Group Conferring β-Lactam Resistance: A Compendium of Phylogenetic Insights from Biochemical, Molecular, and Structural Biology.

Jacinta Mendonça, Carla Guedes, Carina Silva, Sara Sá, Marco Oliveira, Gustavo Accioly, Pilar Baylina, Pedro Barata, Cláudia Pereira, Ruben Fernandes

Open access · goldAbstract read
In one paragraph

Article in Biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 28% of its field
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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. NMR crystallography reveals active-site protonation states of Toho-1 β-lactamase in complex with avibactam.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Outbreak Caused by VIM-1- and VIM-4-PositivePathogens (Basel, Switzerland) · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Beta-Lactam Antibiotic Resistance Genes in the Microbiome of the Public Transport System of Quito, Ecuador.International journal of environmental research and public health · 2023
    Article
  13. 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

10 authors at 3 institutions in 2 countries.

Jacinta MendonçaLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.ORCID 0000-0001-5817-6226
Carla GuedesLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.ORCID 0000-0002-3277-7821
Carina SilvaLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.ORCID 0000-0003-1711-0858
Sara SáLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.ORCID 0000-0002-1376-2624
Marco OliveiraLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.
Gustavo AcciolyESS-Escola Superior de Saúde, IPP-Porto Polytechnic Institute, 4200-072 Porto, Portugal.
Pilar BaylinaLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.ORCID 0000-0002-3740-862X
Pedro BarataLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.ORCID 0000-0002-4537-5450
Cláudia PereiraLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.
Ruben FernandesLABMI-Laboratory of Medical and Industrial Biotechnology, 4200-374 Porto, Portugal.ORCID 0000-0001-8933-3984
Universidade do Porto · PTFernando Pessoa University · PTPolytechnic Institute of Porto · PT

Funding

Fundação para a Ciência e Tecnologia FEDER/02/SAICT/2020/072560Fundação para a Ciência e Tecnologia Norte-01-0145-FEDER-000012
6 · The paper itself

Abstract

The production of extended-spectrum β-lactamases (ESBLs) is the main defense mechanism found in Gram negative bacteria. Among all the ESBLs, the CTX-M enzymes appear as the most efficient in terms of dissemination in different epidemiological contexts. CTX-M enzymes exhibit a striking plasticity, with a large number of allelic variants distributed in several sublineages, which can be associated with functional heterogeneity of clinical relevance. This observational analytical study provides an update of this family, currently with more than 200 variants described, from a phylogenetic, molecular, and structural point of view through homology in amino acid sequences. Our data, combined with described literature, provide phylogenetic and structural evidence of a new group. Thus, herein, we propose six groups among CTX-M enzymes: the already stablished CTX-M-1, CTX-M-2, CTX-M-8, CTX-M-9, and CTX-M-25 clusters, as well as CTX-M-151 as the new cluster.

Indexed as

CTX-M-151 new groupCTX-M β-lactamasesextended-spectrum β-lactamases (ESBL)

Identifiers

PMID35205122
PMCPMC8869216
OpenAlexW4210899110

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.