Evidence map›Paper›PMID 23158101›Full record

ArticleVirology2013

Contribution of SAM and HD domains to retroviral restriction mediated by human SAMHD1.

Tommy E White, Alberto Brandariz-Nuñez, Jose Carlos Valle-Casuso, Sarah Amie, Laura Nguyen, Baek Kim, Jurgen Brojatsch, Felipe Diaz-Griffero

Abstract read
In one paragraph

Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
7.5field-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

98 citing papers in PubMed, 140 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

38 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

8 authors at 2 institutions in 1 country.

Tommy E WhiteDepartment of Microbiology and Immunology, Albert Einstein College of Medicine Bronx, NY 10461, USA.
Alberto Brandariz-Nuñez
Jose Carlos Valle-Casuso
Sarah Amie
Laura Nguyen
Baek Kim
Jurgen Brojatsch
Felipe Diaz-Griffero
Albert Einstein College of Medicine · USUniversity of Rochester · US

Funding

Role of Cellular Factors in Retroviral Uncoating and Synthesis of Viral DNAR01AI087390 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI DIAZ-GRIFFERO, FELIPE · 2010 to 2024
$6.8M
Replication fidelity and lentiviral pathogenesisR01AI049781 · NIAID · UNIVERSITY OF ROCHESTER · PI KIM, BAEK · 2002 to 2016
$4.9M
Training in Cellular, Biochemical and Molecular SciencesT32GM068411 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 2005 to 2019
$3.9M
Role of the B-box-v-1 Restriction by TRIM5alpha proteinsR00MH086162 · NIMH · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI DIAZ-GRIFFERO, FELIPE · 2010 to 2011
$496k
NIAID NIH HHS R01 AI049781NIAID NIH HHS R01 AI087390NIAID NIH HHS R01AI087390NIGMS NIH HHS T32 GM068411NIMH NIH HHS 4R00MH086162-02NIMH NIH HHS R00 MH086162
6 · The paper itself

Abstract

The human SAMHD1 protein is a novel retroviral restriction factor expressed in myeloid cells. Previous work has correlated the deoxynucleotide triphosphohydrolase activity of SAMHD1 with its ability to block HIV-1 and SIV(mac) infection. SAMHD1 is comprised of the sterile alpha motif (SAM) and histidine-aspartic (HD) domains; however the contribution of these domains to retroviral restriction is not understood. Mutagenesis and deletion studies revealed that expression of the sole HD domain of SAMHD1 is sufficient to achieve potent restriction of HIV-1 and SIV(mac). We demonstrated that the HD domain of SAMHD1 is essential for the ability of SAMHD1 to oligomerize by using a biochemical assay. In agreement with previous observations, we mapped the RNA-binding ability of SAMHD1 to the HD domain. We also demonstrated a direct interaction of SAMHD1 with RNA by using enzymatically-active purified SAMHD1 protein from insect cells. Interestingly, we showed that double-stranded RNA inhibits the enzymatic activity of SAMHD1 in vitro suggesting the possibility that RNA from a pathogen might modulate the enzymatic activity of SAMHD1 in cells. By contrast, we found that the SAM domain is dispensable for retroviral restriction, oligomerization and RNA binding. Finally we tested the ability of SAMHD1 to block the infection of retroviruses other than HIV-1 and SIV(mac). These results showed that SAMHD1 blocks infection of HIV-2, feline immunodeficiency virus (FIV), bovine immunodeficiency virus (BIV), Equine infectious anemia virus (EIAV), N-tropic murine leukemia virus (N-MLV), and B-tropic murine leukemia virus (B-MLV).

Indexed as

Cell LineDendritic CellsGreen Fluorescent ProteinsHEK293 CellsHeLa CellsHIV-1HIV-2HumansImmunodeficiency Virus, BovineImmunodeficiency Virus, FelineInfectious Anemia Virus, EquineLeukemia Virus, MurineMacrophagesMonomeric GTP-Binding ProteinsProtein Interaction Domains and MotifsProtein Structure, TertiaryGreen Fluorescent ProteinsMonomeric GTP-Binding ProteinsRecombinant ProteinsRNA-Binding ProteinsRNA, Double-StrandedRNA, ViralSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, human

Identifiers

PMID23158101
PMCPMC3767443
OpenAlexW2088806505

What OpenQuestion holds

Textmetadata
LicenceTDM
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.