Evidence map›Paper›PMID 38922559›Full record

ArticleMarine biotechnology (New York, N.Y.)2024

A Novel Beta-Defensin Isoform from Malabar Trevally, Carangoides malabaricus (Bloch & Schneider, 1801), an Arsenal Against Fish Bacterial Pathogens: Molecular Characterization, Recombinant Production, and Mechanism of Action.

Athira P P, Anju M V, Anooja V V, Archana K, Neelima S, Muhammed Musthafa S, I S Bright Singh, Rosamma Philip

Abstract read
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In one paragraph

Article in Marine biotechnology (New York, N.Y.), 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
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.

  1. Review
  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

8 authors.

Athira P PDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Anju M VDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Anooja V VDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Archana KDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Neelima SDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Muhammed Musthafa SDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
I S Bright SinghNational Centre for Aquatic Animal Health, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Rosamma PhilipDepartment of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India. rosammap@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides (AMPs), including beta-defensin from fish, are a crucial class of peptide medicines. The focus of the current study is the molecular and functional attributes of CmDef, a 63-amino acid beta-defensin AMP from Malabar trevally, Carangoides malabaricus. This peptide demonstrated typical characteristics of AMPs, including hydrophobicity, amphipathic nature, and +2.8 net charge. The CmDef was recombinantly expressed and the recombinant peptide, rCmDef displayed a strong antimicrobial activity against bacterial fish pathogens with an MIC of 8 µM for V. proteolyticus and 32 µM for A. hydrophila. The E. tarda and V. harveyi showed an inhibition of 94% and 54%, respectively, at 32 µM concentration. No activity was observed against V. fluvialis and V. alginolyticus. The rCmDef has a multimode of action that exerts an antibacterial effect by membrane depolarization followed by membrane permeabilization and ROS production. rCmDef also exhibited anti-cancer activities in silico without causing hemolysis. The peptide demonstrated stability under various conditions, including different pH levels, temperatures, salts, and metal ions (KCl and CaCl

Indexed as

beta-DefensinsRecombinant ProteinsAmino Acid SequenceAnimalsAnti-Bacterial AgentsAntimicrobial PeptidesFish DiseasesFish ProteinsHemolysisHumansMicrobial Sensitivity TestsVibrioAnti-Bacterial AgentsAntimicrobial Peptidesbeta-DefensinsFish ProteinsRecombinant ProteinsAntimicrobial peptidesBeta-defensinCarangoides malabaricusFish AMPsMalabar trevally

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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.