ArticleVeterinary research2026
Receptor identification and in vivo efficacy of a lytic phage vB_EcoStr-FJ63A against colistin-resistant Escherichia coli.
Article in Veterinary research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
Bacteriophages (phages), as natural predators of bacteria, represent promising alternatives to antibiotics. However, challenges such as narrow host range and insufficient pharmacokinetic and pharmacodynamic (PK/PD) studies restrict phage therapy. In previous work, we isolated Escherichia phage vB_EcoStr-FJ63A, which exhibits a lytic activity against colistin-resistant Escherichia coli and obvious antibacterial activity in vitro. To elucidate its infection mechanism and evaluate its therapeutic potential, this study focused on identifying its host receptors and assessing its in vivo efficacy. By screening resistant mutants and analyzing the function of mutant sites, we hypothesized that outer membrane proteins (OMPs), lipopolysaccharide (LPS), or extracellular polysaccharides likely serve as receptor candidates for phage vB_EcoStr-FJ63A. The role of LPS as the receptor was supported by competitive binding and receptor removal assays, which demonstrated its necessity for phage adsorption. Bioinformatics analysis results provide evidences for long tail fiber adhesin of phage vB_EcoStr-FJ63A reversibly binds to OmpC, while its short tail fibers irreversibly anchor to LPS. Subsequent PK experiment in healthy mice revealed that a single intraperitoneal injection of phage vB_EcoStr-FJ63A (5 × 10
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.