Evidence map›Paper›PMID 28782023›Full record

ArticleScience advances2017

A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.

Tina Motwani, Ravi K Lokareddy, Carmen A Dunbar, Juliana R Cortines, Martin F Jarrold, Gino Cingolani, Carolyn M Teschke

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Formation and role of the portal ofbioRxiv : the preprint server for biology · 2026
    Article
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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 at 3 institutions in 2 countries.

Tina MotwaniDepartment of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Storrs, CT 06269, USA.
Ravi K LokareddyDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA.
Carmen A DunbarDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405, USA.
Juliana R CortinesDepartment of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Storrs, CT 06269, USA.
Martin F JarroldDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405, USA.
Gino CingolaniDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107, USA.
Carolyn M TeschkeDepartment of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Storrs, CT 06269, USA.
University of Connecticut · USIndiana University Bloomington · USThomas Jefferson University · US

Funding

Understanding the Protein:Protein Interactions Required for Virus AssemblyR01GM076661 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI TESCHKE, CAROLYN M · 2007 to 2022
$7.2M
Multisubunit viral ATPases that couple ATP-hydrolysis to genome translocationR01GM100888 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI CINGOLANI, GINO · 2012 to 2020
$2.5M
NIGMS NIH HHS R01 GM076661NIGMS NIH HHS R01 GM100888
6 · The paper itself

Abstract

Most double-stranded DNA viruses package genetic material into empty precursor capsids (or procapsids) through a dodecameric portal protein complex that occupies 1 of the 12 vertices of the icosahedral lattice. Inhibiting incorporation of the portal complex prevents the formation of infectious virions, making this step an excellent target for antiviral drugs. The mechanism by which a sole portal assembly is selectively incorporated at the special vertex is unclear. We recently showed that, as part of the DNA packaging process for bacteriophage P22, the dodecameric procapsid portal changes conformation to a mature virion state. We report that preformed dodecameric rings of P22 portal protein, as opposed to portal monomers, incorporate into nascent procapsids, with preference for the procapsid portal conformation. Finally, a novel role for P22 scaffolding protein in triggering portal ring formation from portal monomers is elucidated and validated by incorporating de novo assembled portal rings into procapsids.

Indexed as

Protein MultimerizationVirus AssemblyBacteriophage P22Capsid ProteinsModels, MolecularProtein ConformationSpectrum AnalysisViral ProteinsCapsid Proteinsportal protein, bacteriophage P22Viral Proteins

Identifiers

PMID28782023
PMCPMC5529062
OpenAlexW2737241611

What OpenQuestion holds

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LicenceCC BY-NC
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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.