Evidence map›Paper›PMID 31291580›Full record

ArticleCell reports2019

Conserved Herpesvirus Protein Kinases Target SAMHD1 to Facilitate Virus Replication.

Kun Zhang, Dong-Wen Lv, Renfeng Li

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  10. Regulatory mimicry of cyclin-dependent kinases by a conserved herpesvirus protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Transcriptomic Analysis Reveals Key Pathways Influenced by HIV-2 Vpx.International journal of molecular sciences · 2025
    Article
  12. Review
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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

3 authors at 1 institution in 1 country.

Kun ZhangPhilips Institute for Oral Health Research, School of Dentistry, Virginia Commonwealth University, Richmond, VA, USA.
Dong-Wen LvPhilips Institute for Oral Health Research, School of Dentistry, Virginia Commonwealth University, Richmond, VA, USA.
Renfeng LiPhilips Institute for Oral Health Research, School of Dentistry, Virginia Commonwealth University, Richmond, VA, USA; Department of Microbiology and Immunology, School of Medicine, Virginia Commonwealth University, Richmond, VA, USA; Massey Cancer Center, Virginia Commonwealth University, Richmond, VA 23298, USA. Electronic address: rli@vcu.edu.
Virginia Commonwealth University · US

Funding

Virus Vector Shared ResourceP30CA016059 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Kim Felder Rhoads · 1985 to 2026
$51.0M
The Role of PIAS1 in EBV BiologyR01AI141410 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI LI, RENFENG · 2019 to 2023
$1.9M
Impact of herpesvirus protein kinases on host protein modificationR00AI104828 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI LI, RENFENG · 2014 to 2015
$490k
Impact of herpesvirus protein kinases on host protein modificationK99AI104828 · NIAID · JOHNS HOPKINS UNIVERSITY · PI LI, RENFENG · 2013 to 2013
$85k
NCI NIH HHS P30 CA016059NIAID NIH HHS K99 AI104828NIAID NIH HHS R00 AI104828NIAID NIH HHS R01 AI141410
6 · The paper itself

Abstract

To ensure a successful infection, herpesviruses have developed elegant strategies to counterbalance the host anti-viral responses. Sterile alpha motif and HD domain 1 (SAMHD1) was recently identified as an intrinsic restriction factor for a variety of viruses. Aside from HIV-2 and the related simian immunodeficiency virus (SIV) Vpx proteins, the direct viral countermeasures against SAMHD1 restriction remain unknown. Using Epstein-Barr virus (EBV) as a primary model, we discover that SAMHD1-mediated anti-viral restriction is antagonized by EBV BGLF4, a member of the conserved viral protein kinases encoded by all herpesviruses. Mechanistically, we find that BGLF4 phosphorylates SAMHD1 and thereby inhibits its deoxynucleotide triphosphate triphosphohydrolase (dNTPase) activity. We further demonstrate that the targeting of SAMHD1 for phosphorylation is a common feature shared by beta- and gamma-herpesviruses. Together, our findings uncover an immune evasion mechanism whereby herpesviruses exploit the phosphorylation of SAMHD1 to thwart host defenses.

Indexed as

HerpesviridaeHumansProtein KinasesSAM Domain and HD Domain-Containing Protein 1Viral ProteinsVirus ReplicationProtein KinasesSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanViral Proteinsconserved herpesvirus protein kinasescytomegalovirusdNTPaseEpstein-Barr virusinfectionlytic replicationphosphorylationreactivationrestriction factorSAMHD1

Identifiers

PMID31291580
PMCPMC6668718
OpenAlexW2958279351

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.