Evidence map›Paper›PMID 39739874›Full record

ArticleThe Journal of infectious diseases2025

Phage-Encoded Virulence Factor, Gp05, Alters Membrane Phospholipids and Reduces Antimicrobial Susceptibility in Methicillin-Resistant Staphylococcus aureus.

Yi Li, Nagendra N Mishra, Liang Chen, Adhar C Manna, Ambrose L Cheung, Richard A Proctor, Yan Q Xiong

Abstract read
In one paragraph

Article in The Journal of infectious diseases, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Yi LiLundquist Institute for Biomedical Innovation, Harbor-University of California, Los Angeles Medical Center, Torrance.
Nagendra N MishraLundquist Institute for Biomedical Innovation, Harbor-University of California, Los Angeles Medical Center, Torrance.
Liang ChenSchool of Pharmacy and Pharmaceutical Sciences, University at Buffalo, New York.ORCID 0000-0001-5845-2235
Adhar C MannaDepartment of Microbiology & Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire.
Ambrose L CheungDepartment of Microbiology & Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire.
Richard A ProctorDepartments of Medicine and Medical Microbiology/Immunology, University of Wisconsin School of Medicine and Public Health, Madison.
Yan Q XiongLundquist Institute for Biomedical Innovation, Harbor-University of California, Los Angeles Medical Center, Torrance.

Funding

The role of purine biosynthesis and stringent response in persistent MRSA endovascular infectionsR01AI139244 · NIAID · LUNDQUIST INSTITUTE FOR BIOMEDICAL INNOVATION AT HARBOR-UCLA MEDICAL CENTER · PI XIONG, YAN Q. · 2019 to 2023
$2.2M
NIAID NIH HHS R01 AI139244NIH HHS R01 AI139244
6 · The paper itself

Abstract

backgroundMethicillin-resistant Staphylococcus aureus (MRSA) is a leading cause of endovascular infections. The prophage-encoded protein Gp05 has been identified as a critical virulence factor that contributes to MRSA persistence during vancomycin treatment in an experimental endocarditis model. However, the mechanisms underlying this persistence phenotype remain poorly understood.

methodsThis study investigated the genetic factors contributing to Gp05-associated MRSA persistence utilizing RNA sequencing (RNA-seq) on an isogenic MRSA strain set, including a clinical persistent bacteremia isolate, its chromosomal gp05 deletion mutant, and gp05-complemented strains.

resultsRNA-seq revealed significant downregulation of the GraSR two-component regulatory system and its downstream genes, mprF and dltABCD, in the gp05 deletion mutant compared to the wild-type and gp05-complemented strains. This downregulation led to a substantial shift in membrane phospholipid composition, with an increased phosphatidylglycerol and a corresponding decrease in lysyl-phosphatidylglycerol. These changes resulted in increased susceptibility of the gp05 deletion mutant to human cationic antimicrobial peptide (CAMP) LL-37, neutrophils, and vancomycin. These results were confirmed in an isogenic gp05 overexpression strain set in MRSA JE2 background.

conclusionsGp05 modulates MRSA surface phospholipid components and charge, offering new insights into the molecular mechanisms underlying Gp05-mediated persistence in endovascular infections and potential therapeutic targets to combat these infections.

Indexed as

Anti-Bacterial AgentsMethicillin-Resistant Staphylococcus aureusPhospholipidsViral ProteinsVirulence FactorsBacterial ProteinsBacteriophagesGene Expression Regulation, BacterialHumansMicrobial Sensitivity TestsStaphylococcal InfectionsVancomycinAnti-Bacterial AgentsBacterial ProteinsPhospholipidsVancomycinViral ProteinsVirulence FactorsMRSAphage-encoded virulence factorphospholipidstwo-component regulatory systemvancomycin persistence

Identifiers

PMID39739874
PMCPMC12247831

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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.