Evidence map›Paper›PMID 23133382›Full record

ArticlePLoS pathogens2012

A Hsp40 chaperone protein interacts with and modulates the cellular distribution of the primase protein of human cytomegalovirus.

Yonggang Pei, Wenmin Fu, Ed Yang, Ao Shen, Yuan-Chuan Chen, Hao Gong, Jun Chen, Jun Huang, Gengfu Xiao, Fenyong Liu

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

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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

10 authors at 2 institutions in 2 countries.

Yonggang PeiState Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Wenmin Fu
Ed Yang
Ao Shen
Yuan-Chuan Chen
Hao Gong
Jun Chen
Jun Huang
Gengfu Xiao
Fenyong Liu
Wuhan University · CNUniversity of California, Berkeley · US

Funding

Cytomegalovirus virulence in immunodeficient hostsR01AI050468 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI LIU, FENYONG · 2002 to 2013
$3.4M
Cytomegalovirus Infections in Oral CavityR01DE014145 · NIDCR · UNIVERSITY OF CALIFORNIA BERKELEY · PI LIU, FENYONG · 2001 to 2009
$2.7M
NIAID NIH HHS R01 AI050468NIAID NIH HHS R01-AI050468NIDCR NIH HHS R01 DE014145NIDCR NIH HHS R01-DE014145
6 · The paper itself

Abstract

Genomic DNA replication is a universal and essential process for all herpesvirus including human cytomegalovirus (HCMV). HCMV UL70 protein, which is believed to encode the primase activity of the viral DNA replication machinery and is highly conserved among herpesviruses, needs to be localized in the nucleus, the site of viral DNA synthesis. No host factors that facilitate the nuclear import of UL70 have been reported. In this study, we provided the first direct evidence that UL70 specifically interacts with a highly conserved and ubiquitously expressed member of the heat shock protein Hsp40/DNAJ family, DNAJB6, which is expressed as two isoforms, a and b, as a result of alternative splicing. The interaction of UL70 with a common region of DNAJB6a and b was identified by both a two hybrid screen in yeast and coimmunoprecipitation in human cells. In transfected cells, UL70 was primarily co-localized with DNAJB6a in the nuclei and with DNAJB6b in the cytoplasm, respectively. The nuclear import of UL70 was increased in cells in which DNAJB6a was up-regulated or DNAJB6b was down-regulated, and was reduced in cells in which DNAJB6a was down-regulated or DNAJB6b was up-regulated. Furthermore, the level of viral DNA synthesis and progeny production was increased in cells in which DNAJB6a was up-regulated or DNAJB6b was down-regulated, and was reduced in cells in which DNAJB6a was down-regulated or DNAJB6b was up-regulated. Thus, DNAJB6a and b appear to enhance the nuclear import and cytoplasmic accumulation of UL70, respectively. Our results also suggest that the relative expression levels of DNAJB6 isoforms may play a key role in regulating the cellular localization of UL70, leading to modulation of HCMV DNA synthesis and lytic infection.

Indexed as

Alternative SplicingAnimalsCell NucleusCytomegalovirusCytomegalovirus InfectionsDNA PrimaseDNA, ViralHeLa CellsHSP40 Heat-Shock ProteinsHumansMiceMice, Inbred BALB CMolecular ChaperonesNerve Tissue ProteinsProtein BindingViral ProteinsDNAJB6 protein, humanDNA PrimaseDNA, ViralHSP40 Heat-Shock ProteinsMolecular ChaperonesNerve Tissue ProteinsViral Proteins

Identifiers

PMID23133382
PMCPMC3486897
OpenAlexW2109796044

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.