Evidence map›Paper›PMID 34895309›Full record

ArticleParasites & vectors2021

Drug targeting of aminoacyl-tRNA synthetases in Anopheles species and Aedes aegypti that cause malaria and dengue.

Soumyananda Chakraborti, Jyoti Chhibber-Goel, Amit Sharma

Open access · goldAbstract read
In one paragraph

Article in Parasites & vectors, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
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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

3 authors at 2 institutions in 1 country.

Soumyananda Chakraborti *Molecular Medicine Group, National Institute of Malaria Research, New Delhi, India. soumyabiochem@gmail.com.ORCID http://orcid.org/0000-0002-7384-690X
Jyoti Chhibber-Goel *Molecular Medicine, International Centre for Genetic Engineering and Biotechnology, New Delhi, India.
Amit SharmaMolecular Medicine Group, National Institute of Malaria Research, New Delhi, India.
International Centre for Genetic Engineering and Biotechnology · INNational Institute of Malaria Research · IN

Funding

Department of Biotechnology , Ministry of Science and Technology BT/PR30603/BIC/101/1104/2018Department of Biotechnology , Ministry of Science and Technology BT/RLF/Re-entry/09/2019Department of Science and Technology, Ministry of Science and Technology JCB-41
6 · The paper itself

Abstract

backgroundMosquito-borne diseases have a devastating impact on human civilization. A few species of Anopheles mosquitoes are responsible for malaria transmission, and while there has been a reduction in malaria-related deaths worldwide, growing insecticide resistance is a cause for concern. Aedes mosquitoes are known vectors of viral infections, including dengue, yellow fever, chikungunya, and Zika. Aminoacyl-tRNA synthetases (aaRSs) are key players in protein synthesis and are potent anti-infective drug targets. The structure-function activity relationship of aaRSs in mosquitoes (in particular, Anopheles and Aedes spp.) remains unexplored.

methodsWe employed computational techniques to identify aaRSs from five different mosquito species (Anopheles culicifacies, Anopheles stephensi, Anopheles gambiae, Anopheles minimus, and Aedes aegypti). The VectorBase database ( https://vectorbase.org/vectorbase/app ) and web-based tools were utilized to predict the subcellular localizations (TargetP-2.0, UniProt, DeepLoc-1.0), physicochemical characteristics (ProtParam), and domain arrangements (PfAM, InterPro) of the aaRSs. Structural models for prolyl (PRS)-, and phenylalanyl (FRS)-tRNA synthetases-were generated using the I-TASSER and Phyre protein modeling servers.

resultsAmong the vector species, a total of 37 (An. gambiae), 37 (An. culicifacies), 37 (An. stephensi), 37 (An. minimus), and 35 (Ae. aegypti) different aaRSs were characterized within their respective mosquito genomes. Sequence identity amongst the aaRSs from the four Anopheles spp. was > 80% and in Ae. aegypti was > 50%.

conclusionsStructural analysis of two important aminoacyl-tRNA synthetases [prolyl (PRS) and phenylanalyl (FRS)] of Anopheles spp. suggests structural and sequence similarity with potential antimalarial inhibitor [halofuginone (HF) and bicyclic azetidine (BRD1369)] binding sites. This suggests the potential for repurposing of these inhibitors against the studied Anopheles spp. and Ae. aegypti.

Indexed as

AedesAmino Acid SequenceAmino Acyl-tRNA SynthetasesAnimalsAnophelesDengueDrug Delivery SystemsDrug DiscoveryGenomicsHumansInsecticide ResistanceInsecticidesMalariaModels, StructuralMosquito VectorsSequence AlignmentAmino Acyl-tRNA SynthetasesInsecticidesAedes spp.Aminoacyl-tRNA synthetasesAnopheles spp.Drug discoveryGenomics

Identifiers

PMID34895309
PMCPMC8665550
OpenAlexW4200252761

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.