Evidence map›Paper›PMID 32725318›Full record

ArticleJournal, genetic engineering & biotechnology2020

Prioritization of Mur family drug targets against A. baumannii and identification of their homologous proteins through molecular phylogeny, primary sequence, and structural analysis.

Gizachew Muluneh Amera, Rameez Jabeer Khan, Rajat Kumar Jha, Amita Pathak, Jayaraman Muthukumaran, Amit Kumar Singh

Open access · diamondAbstract read
In one paragraph

Article in Journal, genetic engineering & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 51% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Gizachew Muluneh AmeraDepartment of Biotechnology, School of Engineering and Technology, Sharda University, Greater Noida, UP, 201310, India.
Rameez Jabeer KhanDepartment of Biotechnology, School of Engineering and Technology, Sharda University, Greater Noida, UP, 201310, India.
Rajat Kumar JhaDepartment of Biotechnology, School of Engineering and Technology, Sharda University, Greater Noida, UP, 201310, India.
Amita PathakDepartment of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi, 110016, India.
Jayaraman MuthukumaranDepartment of Biotechnology, School of Engineering and Technology, Sharda University, Greater Noida, UP, 201310, India.
Amit Kumar SinghDepartment of Biotechnology, School of Engineering and Technology, Sharda University, Greater Noida, UP, 201310, India. amitk.singh@sharda.ac.in.
Sharda University · INIndian Institute of Technology Delhi · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe World Health Organization (WHO) report stated that Acinetobacter baumannii had been classified as one of the most important pathogenic bacteria causing nosocomial infection in hospital patients due to multi-drug resistance (MDR). It is vital to find out new bacterial drug targets and annotated their structure and function for the exploration of new anti-bacterial agents. The present study utilized a systematic route to prioritize the potential drug targets that belong to Mur family of Acinetobacter baumannii and identify their homologous proteins using a computational approach such as sequence similarity search, multiple sequence alignment, phylogenetic analysis, protein sequence, and protein structure analysis.

resultsFrom the results of protein sequence analysis of eight Mur family proteins, they divided into three main enzymatic classes namely transferases (MurG, MurA and MraY), ligases (MurC, MurD, MurE, and MurF), and oxidoreductase (MurB). Based on the results of intra-comparative protein sequence analysis and enzymatic classification, we have chosen MurB, MurE, and MurG as the prioritized drug targets from A. baumannii and subjected them for further detailed studies of inter-species comparison. This inter-species comparison help us to explore the sequential and structural properties of homologous proteins in other species and hence, opens a gateway for new target identification and using common inhibitor for different bacterial species caused by various diseases. The pairwise sequence alignment results between A. baumannii's MurB with A. calcoaceticus's MurB, A. baumannii's MurE with A. seifertii's MurE, and A. baumannii's MurG with A. pittii's MurG showed that every group of the proteins are highly similar with each other and they showed sequence identity of 95.7% and sequence similarity of 97.2%.

conclusionTogether with the results of secondary and three-dimensional structure predictions explained that three selected proteins (MurB, MurE, and MurG) from A. baumannii and their related proteins (AcMurB, AsMurE, and ApMurG) belong to mixed αβ class and they are very similar.

Indexed as

3D structureAcinetobacter baumanniiDrug targets Secondary structureMolecular phylogenyPrimary sequence

Identifiers

PMID32725318
PMCPMC7387395
OpenAlexW3045823453

What OpenQuestion holds

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Registered trials

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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.