Evidence map›Paper›PMID 25816773›Full record

ArticleJournal of molecular biology2015

Key residues of S. flexneri OmpA mediate infection by bacteriophage Sf6.

Natalia B Porcek, Kristin N Parent

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. TheJournal of virology · 2025
    Article
  2. Moo19 and B2: Structures ofScience advances · 2024
    Article
  3. Comparative Genomics of Six LyticPHAGE (New Rochelle, N.Y.) · 2022
    Article
  4. Host Range Expansion ofJournal of virology · 2022
    Article
  5. Review
  6. Article
  7. Mosaic Evolution of Beta-Barrel-Porin-Encoding Genes inApplied and environmental microbiology · 2022
    Article
  8. Article
  9. Article
  10. Ecology, Structure, and Evolution ofAnnual review of virology · 2020
    Review
  11. Screening of Polyvalent Phage-ResistantFrontiers in microbiology · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The outer-membrane protein TolC ofThe Journal of biological chemistry · 2018
    Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

Natalia B PorcekMichigan State University Department of Microbiology and Molecular Genetics, East Lansing, MI 48824, USA; Michigan State University Department of Biochemistry and Molecular Biology, East Lansing, MI 48824, USA.
Kristin N ParentMichigan State University Department of Biochemistry and Molecular Biology, East Lansing, MI 48824, USA.
Michigan State University · US

Funding

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 GM110185
6 · The paper itself

Abstract

Many viruses, including bacteriophage, have the inherent ability to utilize several types of proteinaceous receptors as an attachment mechanism to infect cells, yet the molecular mechanisms that drive receptor binding have not been elucidated. Using bacteriophage Sf6 and its host, Shigella flexneri, we investigated how Sf6 utilizes outer membrane protein A (OmpA) for infection. Specifically, we identified that surface loops of OmpA mediate Shigella infection. We further characterized which residues in the surface loops are responsible for Sf6 binding and productive infection using a combination of in vivo and in vitro approaches including site-directed mutagenesis, phage plaque assays, circular dichroism spectroscopy, and in vitro genome ejection assays. Our data indicate that Sf6 can productively interact with other bacterial OmpAs as long as they share homology in loops 2 and 4, suggesting that these loops may determine host specificity. Our data provide a model in which Sf6 interacts with OmpA using the surface of the protein and new insights into viral attachment through binding to membrane protein receptors.

Indexed as

Amino Acid SubstitutionBacterial Outer Membrane ProteinsBacteriophagesCircular DichroismDNA, ViralGenome, ViralMutagenesis, Site-DirectedMutationShigella flexneriVirionBacterial Outer Membrane ProteinsDNA, ViralOMPA outer membrane proteinscircular dichroismouter membrane proteinsphage attachmentplaque assayvirus receptor

Identifiers

PMID25816773
PMCPMC7670968
OpenAlexW2073619306

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.