Evidence map›Paper›PMID 20023299›Full record

ArticleMolecular & cellular proteomics : MCP2010

A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation.

Nathaniel J Moorman, Ronit Sharon-Friling, Thomas Shenk, Ileana M Cristea

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

75 citing papers in PubMed, 96 citations in OpenAlex.

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15 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Nathaniel J MoormanDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
Ronit Sharon-Friling
Thomas Shenk
Ileana M Cristea
Princeton University · US

Funding

HUMAN CYTOMEGALOVIRUS TEGUMENT PROTEINSR01CA082396 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 1999 to 2013
$5.0M
Proteomic Tools to Uncover the Role of Chromatin Remodeling in HIV-1 InfectionDP1DA026192 · NIDA · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 2008 to 2012
$3.9M
CYTOMEGALOVIRUS IMMEDIATE EARLY PROTEINS AND VIRION RNASR01CA085786 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 2000 to 2010
$3.7M
NCI NIH HHS CA82396NCI NIH HHS CA85786NCI NIH HHS R01 CA082396NCI NIH HHS R01 CA085786NIDA NIH HHS DP1 DA026192NIDA NIH HHS DP1DA026192
6 · The paper itself

Abstract

The assembly of infectious virus particles is a complex event. For human cytomegalovirus (HCMV) this process requires the coordinated expression and localization of at least 60 viral proteins that comprise the infectious virion. To gain insight into the mechanisms controlling this process, we identified protein binding partners for two viral proteins, pUL99 (also termed pp28) and pUL32 (pp150), which are essential for HCMV virion assembly. We utilized HCMV strains expressing pUL99 or pUL32 carboxyl-terminal green fluorescent protein fusion proteins from their native location in the HCMV genome. Based on the presence of ubiquitin in the pUL99 immunoisolation, we discovered that this viral protein colocalizes with components of the cellular endosomal sorting complex required for transport (ESCRT) pathway during the initial stages of virion assembly. We identified the nucleocapsid and a large number of tegument proteins as pUL32 binding partners, suggesting that events controlling trafficking of this viral protein in the cytoplasm regulate nucleocapsid/tegument maturation. The finding that pUL32, but not pUL99, associates with clathrin led to the discovery that the two viral proteins traffic via distinct pathways during the early stages of virion assembly. Additional investigation revealed that the majority of the major viral glycoprotein gB initially resides in a third compartment. Analysis of the trafficking of these three viral proteins throughout a time course of virion assembly allowed us to visualize their merger into a single large cytoplasmic structure during the late stages of viral assembly. We propose a model of HCMV virion maturation in which multiple components of the virion traffic independently of one another before merging.

Indexed as

Virus AssemblyAmino Acid SequenceBrefeldin ACell CompartmentationClathrinCytomegalovirusEndosomal Sorting Complexes Required for TransportFibroblastsHost-Pathogen InteractionsHumansModels, BiologicalMolecular Sequence DataNucleocapsidProtein BindingProtein TransportProteomicsBrefeldin AClathrinEndosomal Sorting Complexes Required for TransportViral Proteins

Identifiers

PMID20023299
PMCPMC2871419
OpenAlexW2109177153

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.