Evidence map›Paper›PMID 21632759›Full record

ArticleJournal of virology2011

Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage.

Andrei Fokine, Mohammad Z Islam, Zhihong Zhang, Valorie D Bowman, Venigalla B Rao, Michael G Rossmann

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

51 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  5. Moo19 and B2: Structures ofScience advances · 2024
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  12. Review
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  15. Article
  16. International journal of molecular sciences · 2022
    Article
  17. Review
  18. Bacteriophages evolve enhanced persistence to a mucosal surface.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Engineering T4 Bacteriophage forACS synthetic biology · 2021
    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

6 authors at 3 institutions in 1 country.

Andrei FokineDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-2032, USA.
Mohammad Z Islam
Zhihong Zhang
Valorie D Bowman
Venigalla B Rao
Michael G Rossmann
Purdue University West Lafayette · USCatholic University of America · USUniversity of America · US

Funding

Structural studies of bacteriophage T4 and their potential medical applicationsR01AI081726 · NIAID · PURDUE UNIVERSITY · PI KUHN, RICHARD J., RAO, VENIGALLA B. · 2010 to 2019
$6.2M
Phase T4 Head Assembly and Initiation of InfectionR01AI011676 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI BLACK, LINDSAY W · 1985 to 2013
$4.1M
STRUCTURE OF A SMALL SPHERICAL VIRUSR01AI011219 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 1985 to 2020
$2.4M
Multivalent Plague, Anthrax Vaccines Using Bacteriophage T4 DisplayU01AI082086 · NIAID · CATHOLIC UNIVERSITY OF AMERICA · PI RAO, VENIGALLA B. · 2009 to 2013
$2.2M
Potent Phage T4 Derived V2 Immunogens as HIV VaccinesR01AI102725 · NIAID · CATHOLIC UNIVERSITY OF AMERICA · PI RAO, VENIGALLA B. · 2012 to 2015
$1.7M
NIAID NIH HHS AI082086NIAID NIH HHS R01 AI011219NIAID NIH HHS R01 AI011676NIAID NIH HHS R01 AI081726NIAID NIH HHS R01AI081726NIAID NIH HHS R01 AI102725NIAID NIH HHS U01 AI082086
6 · The paper itself

Abstract

The head of bacteriophage T4 is decorated with 155 copies of the highly antigenic outer capsid protein (Hoc). One Hoc molecule binds near the center of each hexameric capsomer. Hoc is dispensable for capsid assembly and has been used to display pathogenic antigens on the surface of T4. Here we report the crystal structure of a protein containing the first three of four domains of Hoc from bacteriophage RB49, a close relative of T4. The structure shows an approximately linear arrangement of the protein domains. Each of these domains has an immunoglobulin-like fold, frequently found in cell attachment molecules. In addition, we report biochemical data suggesting that Hoc can bind to Escherichia coli, supporting the hypothesis that Hoc could attach the phage capsids to bacterial surfaces and perhaps also to other organisms. The capacity for such reversible adhesion probably provides survival advantages to the bacteriophage.

Indexed as

Amino Acid SequenceBacteriophage T4Binding SitesCapsid ProteinsCrystallizationCrystallography, X-RayEscherichia coliMyoviridaeProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsSequence Analysis, ProteinCapsid ProteinsRecombinant Fusion Proteins

Identifiers

PMID21632759
PMCPMC3147960
OpenAlexW2062188115

What OpenQuestion holds

Textmetadata
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.