Evidence map›Paper›PMID 24824860›Full record

ArticleThe Journal of general virology2014

A hydrophobic domain within the small capsid protein of Kaposi's sarcoma-associated herpesvirus is required for assembly.

Christopher M Capuano, Peter Grzesik, Dale Kreitler, Erin N Pryce, Keshal V Desai, Gavin Coombs, J Michael McCaffery, Prashant J Desai

Open access · greenAbstract read
In one paragraph

Article in The Journal of general virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
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  5. 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

8 authors at 3 institutions in 1 country.

Christopher M CapuanoViral Oncology Program, The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD, USA.
Peter GrzesikViral Oncology Program, The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD, USA.
Dale KreitlerViral Oncology Program, The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD, USA.
Erin N PryceIntegrated Imaging Center, Department of Biology, Johns Hopkins University, Baltimore, MD, USA.
Keshal V DesaiViral Oncology Program, The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD, USA.
Gavin CoombsIntegrated Imaging Center, Department of Biology, Johns Hopkins University, Baltimore, MD, USA.
J Michael McCafferyIntegrated Imaging Center, Department of Biology, Johns Hopkins University, Baltimore, MD, USA.
Prashant J DesaiViral Oncology Program, The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins, Baltimore, MD, USA.
Sidney Kimmel Comprehensive Cancer Center · USJohns Hopkins University · USImaging Center · US

Funding

TRANS NETWORK PROJECTSU54CA143868 · NCI · JOHNS HOPKINS UNIVERSITY · PI KONSTANTOPOULOS, KONSTANTINOS · 2009 to 2013
$13.7M
Maturation functions of the HSV-1 tegumentR01AI061382 · NIAID · JOHNS HOPKINS UNIVERSITY · PI DESAI, PRASHANT J · 2006 to 2010
$1.8M
FEI Tecnai 12 BioTWIN Transmission Electron MicroscopeS10RR023454 · NCRR · JOHNS HOPKINS UNIVERSITY · PI MCCAFFERY, J. MICHAEL · 2007 to 2007
$476k
Establish and Apply In Vitro System for Human Cytomegalovirus Capsid AssemblyR21AI097912 · NIAID · JOHNS HOPKINS UNIVERSITY · PI GIBSON, D WADE · 2012 to 2013
$431k
How does the KSHV small capsid protein function to promote self-assembly?R21AI107530 · NIAID · JOHNS HOPKINS UNIVERSITY · PI DESAI, PRASHANT J · 2013 to 2014
$431k
NCI NIH HHS 1U54CA143868-01NCI NIH HHS U54 CA143868NCRR NIH HHS S10 RR023454NCRR NIH HHS S10RR023454-01NIAID NIH HHS R01 AI061382NIAID NIH HHS R21 AI097912NIAID NIH HHS R21 AI107530NIAID NIH HHS R21AI107530
6 · The paper itself

Abstract

Kaposi's sarcoma-associated herpesvirus (KSHV) capsids can be produced in insect cells using recombinant baculoviruses for protein expression. All six capsid proteins are required for this process to occur and, unlike for alphaherpesviruses, the small capsid protein (SCP) ORF65 is essential for this process. This protein decorates the capsid shell by virtue of its interaction with the capsomeres. In this study, we have explored the SCP interaction with the major capsid protein (MCP) using GFP fusions. The assembly site within the nucleus of infected cells was visualized by light microscopy using fluorescence produced by the SCP-GFP polypeptide, and the relocalization of the SCP to these sites was evident only when the MCP and the scaffold protein were also present - indicative of an interaction between these proteins that ensures delivery of the SCP to assembly sites. Biochemical assays demonstrated a physical interaction between the SCP and MCP, and also between this complex and the scaffold protein. Self-assembly of capsids with the SCP-GFP polypeptide was evident. Potentially, this result can be used to engineer fluorescent KSHV particles. A similar SCP-His6 polypeptide was used to purify capsids from infected cell lysates using immobilized affinity chromatography and to directly label this protein in capsids using chemically derivatized gold particles. Additional studies with SCP-GFP polypeptide truncation mutants identified a domain residing between aa 50 and 60 of ORF65 that was required for the relocalization of SCP-GFP to nuclear assembly sites. Substitution of residues in this region and specifically at residue 54 with a polar amino acid (lysine) disrupted or abolished this localization as well as capsid assembly, whereas substitution with non-polar residues did not affect the interaction. Thus, this study identified a small conserved hydrophobic domain that is important for the SCP-MCP interaction.

Indexed as

Virus AssemblyAnimalsCapsid ProteinsCell LineDNA Mutational AnalysisHerpesvirus 8, HumanProtein BindingProtein Structure, TertiaryProtein TransportSpodopteraViral ProteinsCapsid ProteinsORF65 protein, human herpesvirus 8Viral Proteins

Identifiers

PMID24824860
PMCPMC4103069
OpenAlexW2016497066

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.