Evidence map›Paper›PMID 38611711›Full record

ArticleMolecules (Basel, Switzerland)2024

Camel-Derived Nanobodies as Potent Inhibitors of New Delhi Metallo-β-Lactamase-1 Enzyme.

Rahma Ben Abderrazek, Emna Hamdi, Alessandra Piccirilli, Sayda Dhaouadi, Serge Muyldermans, Mariagrazia Perilli, Balkiss Bouhaouala-Zahar

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 95% 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

2 citing papers in PubMed, 0 citations in OpenAlex.

  1. Article
  2. Review
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

7 authors at 4 institutions in 3 countries.

Rahma Ben AbderrazekLaboratoire des Biomolécules Venins et Applications Théranostiques, Institut Pasteur Tunis, 13 Place Pasteur, Tunisie Université Tunis El Manar, B.P N 93, Tunis 1068, Tunisia.
Emna HamdiLaboratoire des Biomolécules Venins et Applications Théranostiques, Institut Pasteur Tunis, 13 Place Pasteur, Tunisie Université Tunis El Manar, B.P N 93, Tunis 1068, Tunisia.ORCID 0009-0007-7272-0225
Alessandra PiccirilliDipartimento di Scienze Cliniche Applicate e Biotecnologiche, Università degli Studi dell'Aquila, Via Veteoio Coppito, 67100 L'Aquila, Italy.
Sayda DhaouadiLaboratoire des Biomolécules Venins et Applications Théranostiques, Institut Pasteur Tunis, 13 Place Pasteur, Tunisie Université Tunis El Manar, B.P N 93, Tunis 1068, Tunisia.
Serge MuyldermansLaboratory of Cellular and Molecular Immunology, Vrije Universiteit Brussel, Pleenlaan, 9, 1050 Brussels, Belgium.ORCID 0000-0002-3678-3575
Mariagrazia PerilliDipartimento di Scienze Cliniche Applicate e Biotecnologiche, Università degli Studi dell'Aquila, Via Veteoio Coppito, 67100 L'Aquila, Italy.ORCID 0000-0001-7370-1455
Balkiss Bouhaouala-ZaharLaboratoire des Biomolécules Venins et Applications Théranostiques, Institut Pasteur Tunis, 13 Place Pasteur, Tunisie Université Tunis El Manar, B.P N 93, Tunis 1068, Tunisia.ORCID 0000-0003-3147-245X
University of L'Aquila · ITInstitut Pasteur de Tunis · TNTunis University · TNVrije Universiteit Brussel · BE

Funding

DISCAB Grant 2023Federative National Project, PRF (D4P1) PRF (D4P1)Internal Collaborative Program PCI-36Project Encouraging Young Researchers 18PEC06-06
6 · The paper itself

Abstract

The injudicious usage of antibiotics during infections caused by Gram-negative bacteria leads to the emergence of β-lactamases. Among them, the NDM-1 enzyme poses a serious threat to human health. Developing new antibiotics or inhibiting β-lactamases might become essential to reduce and prevent bacterial infections. Nanobodies (Nbs), the smallest antigen-binding single-domain fragments derived from Camelidae heavy-chain-only antibodies, targeting enzymes, are innovative alternatives to develop effective inhibitors. The biopanning of an immune VHH library after phage display has helped to retrieve recombinant antibody fragments with high inhibitory activity against recombinant-NDM-1 enzyme. Nb02NDM-1, Nb12NDM-1, and Nb17NDM-1 behaved as uncompetitive inhibitors against NDM-1 with K

Indexed as

CamelusSingle-Domain AntibodiesAnimalsAnti-Bacterial Agentsbeta-LactamasesHumansImmunoglobulin Heavy ChainsAnti-Bacterial Agentsbeta-lactamase NDM-1beta-LactamasesImmunoglobulin Heavy ChainsSingle-Domain Antibodiesmetallo-β-lactamasesnanobodiesNDM-1phage displayβ-lactamase small molecule inhibitors

Identifiers

PMID38611711
PMCPMC11013165
OpenAlexW4393094281

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.