Evidence map›Paper›PMID 41491636›Full record

ArticleMicrobial biotechnology2026

Characterisation of a Novel Jumbo Lytic Aeromonas dhakensis Bacteriophage P19 and Its Endolysin.

Farhat Ansari, Vandan Nagar

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Article in Microbial biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Farhat AnsariFood Technology Division, Bhabha Atomic Research Centre, Mumbai, India.ORCID https://orcid.org/0009-0001-0558-5402
Vandan NagarFood Technology Division, Bhabha Atomic Research Centre, Mumbai, India.ORCID https://orcid.org/0000-0001-6556-8068

Funding

Department of Atomic Energy, Government of India
6 · The paper itself

Abstract

Aeromonas dhakensis is an emerging multidrug-resistant (MDR) bacterial pathogen that presents significant threats to public health and aquaculture. This study reports the isolation and comprehensive characterisation of jumbo bacteriophage P19. It is a lytic phage with a long, contractile tail and is placed in the genus Ceceduovirus of the family Straboviridae. P19 possesses a large genome typical of jumbo phages, which likely contributes to its enhanced replication efficiency and adaptability. P19 exhibited strong lytic activity with a high efficiency of plating (EOP) against multiple A. dhakensis strains, a burst size of approximately 50 plaque-forming units (PFU) per cell, and a latent period of 30 min. It remained highly stable across pH 6-10 and temperatures up to 60°C. Genomic analysis revealed a 228 kb genome with 414 open reading frames (ORFs) and absence of genes related to lysogeny, antibiotic resistance or virulence, indicating its potential for safe therapeutic and biocontrol applications. ORF_358 encodes a stable and soluble T4-type lysozyme endolysin (molecular weight 18.8 kDa) belonging to the glycoside hydrolase family 24. Molecular docking analysis demonstrated strong binding affinity (-6.4 kcal/mol) between P19_358 and the peptidoglycan NAG-NAM dimer. Recombinant P19_358 endolysin exhibited 99.98% relative lytic activity against Gram-positive bacterium Bacillus subtilis at a concentration of 75 μg/mL without EDTA pre-treatment; whereas, it showed broad-spectrum antibacterial activity against several Gram-negative pathogens, including A. dhakensis, Shigella flexneri, Salmonella Typhimurium, Pseudomonas aeruginosa and Escherichia coli, with relative activity ranging from 71% to 97% following pre-treatment with 100 mM EDTA. These findings collectively indicate that phage P19 and its endolysin P19_358 possess potent lytic activity and favourable stability profiles, supporting their development as promising antimicrobial agents against MDR Gram-negative pathogens.

Indexed as

AeromonasBacteriophagesEndopeptidasesEnzyme StabilityGenome, ViralHydrogen-Ion ConcentrationMolecular Docking SimulationOpen Reading FramesTemperatureViral ProteinsendolysinEndopeptidasesViral ProteinsAeromonas dhakensisantibacterial activitybacteriophageendolysingram‐negative bacteria

Identifiers

PMID41491636
PMCPMC12771599

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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.