Evidence map›Paper›PMID 35891382›Full record

ArticleViruses2022

Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22.

Brianna M Woodbury, Tina Motwani, Makayla N Leroux, Lauren F Barnes, Nicholas A Lyktey, Sanchari Banerjee, Corynne L Dedeo, Martin F Jarrold, Carolyn M Teschke

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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

9 authors at 2 institutions in 1 country.

Brianna M WoodburyDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Tina MotwaniDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Makayla N LerouxDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Lauren F BarnesDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405, USA.
Nicholas A LykteyDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405, USA.
Sanchari BanerjeeDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Corynne L DedeoDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.
Martin F JarroldDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405, USA.
Carolyn M TeschkeDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.ORCID 0000-0001-6420-4895
University of Connecticut · USIndiana University Bloomington · 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
Developing High-Resolution Ion Mobility Spectrometry-Charge Detection-Mass Spectrometry for Rapid Analysis in the Megadalton to Gigadalton RegimeR01GM131100 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., JARROLD, MARTIN F · 2019 to 2022
$2.1M
NIGMS NIH HHS R01 GM076661NIGMS NIH HHS R01GM076661NIGMS NIH HHS R01 GM131100NIGMS NIH HHS R01GM131100
6 · The paper itself

Abstract

The oligomerization and incorporation of the bacteriophage P22 portal protein complex into procapsids (PCs) depends upon an interaction with scaffolding protein, but the region of the portal protein that interacts with scaffolding protein has not been defined. In herpes simplex virus 1 (HSV-1), conserved tryptophan residues located in the wing domain are required for portal-scaffolding protein interactions. In this study, tryptophan residues (W) present at positions 41, 44, 207 and 211 within the wing domain of the bacteriophage P22 portal protein were mutated to both conserved and non-conserved amino acids. Substitutions at each of these positions were shown to impair portal function in vivo, resulting in a lethal phenotype by complementation. The alanine substitutions caused the most severe defects and were thus further characterized. An analysis of infected cell lysates for the W to A mutants revealed that all the portal protein variants except W211A, which has a temperature-sensitive incorporation defect, were successfully recruited into procapsids. By charge detection mass spectrometry, all W to A mutant portal proteins were shown to form stable dodecameric rings except the variant W41A, which dissociated readily to monomers. Together, these results suggest that for P22 conserved tryptophan, residues in the wing domain of the portal protein play key roles in portal protein oligomerization and incorporation into procapsids, ultimately affecting the functionality of the portal protein at specific stages of virus assembly.

Indexed as

Bacteriophage P22Herpesvirus 1, HumanCapsidCapsid ProteinsTryptophanVirus AssemblyCapsid ProteinsTryptophanDNA packagingdsDNA virusterminasevirus assembly

Identifiers

PMID35891382
PMCPMC9320234
OpenAlexW4283642382

What Socratic holds

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LicenceCC BY
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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 Socratic graph.