Evidence map›Paper›PMID 35358430›Full record

ArticleBiochimica et biophysica acta. Biomembranes2022

Shigella viruses Sf22 and KRT47 require outer membrane protein C for infection.

Kendal R Tinney, John A Dover, Sarah M Doore, Kristin N Parent

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. New microbes and new infections · 2026
    Review
  2. Article
  3. Moo19 and B2: Structures ofScience advances · 2024
    Article
  4. Host Range Expansion ofJournal of virology · 2022
    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

4 authors at 2 institutions in 1 country.

Kendal R TinneyDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA.
John A DoverDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA.
Sarah M DooreDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA; Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611. Electronic address: sdoore@ufl.edu.
Kristin N ParentDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA. Electronic address: kparent@msu.edu.
Michigan State University · USUniversity of Florida · US

Funding

Bacteriophage interactions with enteric pathogens-the essential role of inner membrane protein YajCR35GM140803 · NIGMS · MICHIGAN STATE UNIVERSITY · PI Kristin N Parent · 2021 to 2026
$2.5M
Sf6 as a model system for understanding the mechanisms of virus: host recognitionR01GM110185 · NIGMS · MICHIGAN STATE UNIVERSITY · PI PARENT, KRISTIN N · 2015 to 2019
$1.4M
NIGMS NIH HHS R01 GM110185NIGMS NIH HHS R35 GM140803
6 · The paper itself

Abstract

Viruses rely on hosts for their replication: thus, a critical step in the infection process is identifying a suitable host cell. Bacterial viruses, known as bacteriophages or phages, often use receptor binding proteins to discriminate between susceptible and non-susceptible hosts. By being able to evade predation, bacteria with modified or deleted receptor-encoding genes often undergo positive selection during growth in the presence of phage. Depending on the specific receptor(s) a phage uses, this may subsequently affect the bacteria's ability to form biofilms, its resistance to antibiotics, pathogenicity, or its phenotype in various environments. In this study, we characterize the interactions between two T4-like phages, Sf22 and KRT47, and their host receptor S. flexneri outer membrane protein C (OmpC). Results indicate that these phages use a variety of surface features on the protein, and that complete resistance most frequently occurs when hosts delete the ompC gene in full, encode premature stop codons to prevent OmpC synthesis, or eliminate specific regions encoding exterior loops.

Indexed as

Bacterial ProteinsBacteriophagesPorinsShigellaVirulenceBacterial ProteinsOmpC proteinPorinsBacteriophageouter membrane protein Cphage-host interactionsPhage therapyShigella

Identifiers

PMID35358430
PMCPMC10037218
OpenAlexW4220807836

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.