Evidence map›Paper›PMID 24725932›Full record

ArticleVirology2014

Nuclear trafficking of the HIV-1 pre-integration complex depends on the ADAM10 intracellular domain.

Mark A Endsley, Anoma D Somasunderam, Guangyu Li, Numan Oezguen, Varatharasa Thiviyanathan, James L Murray, Donald H Rubin, Thomas W Hodge, William A O'Brien, Briana Lewis and 1 more

Abstract read
In one paragraph

Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  9. Article
  10. Regulation of Alpha-Secretase ADAM10Frontiers in molecular neuroscience · 2017
    Review
  11. Review
  12. Article
  13. Review
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

11 authors at 9 institutions in 4 countries.

Mark A EndsleyDepartment Internal Medicine, Division of Infectious Diseases, University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: maendsle@utmb.edu.
Anoma D SomasunderamDepartment Internal Medicine, Division of Infectious Diseases, University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: asomasun@utmb.edu.
Guangyu LiDepartment of Internal Medicine, Quillen College of Medicine, East Tennessee State University, Johnson City, TN 37614, USA. Electronic address: LIG001@mail.etsu.edu.
Numan OezguenDepartment of Pathology & Immunology, Microbiome Center, Texas Children׳s Hospital, Houston, TX 77030, USA. Electronic address: numan.oezguen@bcm.edu.
Varatharasa ThiviyanathanInstitute of Molecular Medicine, University of Texas Health Science Center, Houston, TX 77030, USA. Electronic address: Varatharasa.Thiviyanathan@uth.tmc.edu.
James L MurrayGeneTAG Technology, Inc., 3155 Northwoods Place, Norcross, GA 30071, USA. Electronic address: jmurray100@yahoo.com.
Donald H RubinResearch Medicine, VA Tennessee Valley Healthcare System, 1310 24th Ave. South, Nashville, TN 37212, USA; Departments of Medicine, Pathology, Microbiology & Immunology, Vanderbilt University School of Medicine, 1161 21st Ave South, Nashville, TN 37232, USA. Electronic address: don.h.rubin@vanderbilt.edu.
Thomas W HodgePre-clinical and Antiviral Research, Tamir Biotechnology, Inc., 12625 High Bluff Dr., Suite 113, San Diego, CA 92130, USA. Electronic address: twhodge3@gmail.com.
William A O'BrienDepartment Internal Medicine, Division of Infectious Diseases, University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA; Clinical Development Medical Affairs, Virology, Boehringer Ingelheim, 900 Ridgebury Rd., Ridgefield, CT 06877, USA; Department of Internal Medicine, Division of Infectious Diseases, Emory University School of Medicine, 100 Woodruff Circle, Atlanta, GA 30322, USA. Electronic address: william.obrien@boehringer-ingelheim.com.
Briana LewisDepartment Internal Medicine, Division of Infectious Diseases, University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: br3lewis@utmb.edu.
Monique R FergusonDepartment Internal Medicine, Division of Infectious Diseases, University of Texas Medical Branch, 301 University Blvd, Galveston, TX 77555, USA. Electronic address: mrfergus@utmb.edu.
The University of Texas Medical Branch at Galveston · USBaylor College of Medicine · USBipar · FREast Tennessee State University · USEmory University · USIowa Western Community College · USOFS (United States) · USTexas Medical Center · USVanderbilt University · US

Funding

Virology CoreP30AI036211 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI BUTEL, JANET S · 1994 to 2015
$21.7M
Texas Center for Cancer NanomedicineU54CA151668 · NCI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LOPEZ-BERESTEIN, GABRIEL · 2010 to 2014
$12.4M
Training in Emerging Infectious Diseases and BiodefenseT32AI007536 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI WHITE, ARTHUR CLINTON · 1998 to 2013
$4.1M
Role of Tetraspan Glycoproteins (CD63) in HIV ReplicationR01HL088999 · NHLBI · UNIVERSITY OF TEXAS MED BR GALVESTON · PI FERGUSON, MONIQUE REGAIL · 2006 to 2011
$2.5M
NCI NIH HHS U54 CA151668NHLBI NIH HHS HL088999NHLBI NIH HHS R01 HL088999NIAID NIH HHS AI007536NIAID NIH HHS P30 AI036211NIAID NIH HHS T32 AI007536
6 · The paper itself

Abstract

Previously, we showed that ADAM10 is necessary for HIV-1 replication in primary human macrophages and immortalized cell lines. Silencing ADAM10 expression interrupted the HIV-1 life cycle prior to nuclear translocation of viral cDNA. Furthermore, our data indicated that HIV-1 replication depends on the expression of ADAM15 and γ-secretase, which proteolytically processes ADAM10. Silencing ADAM15 or γ-secretase expression inhibits HIV-1 replication between reverse transcription and nuclear entry. Here, we show that ADAM10 expression also supports replication in CD4(+) T lymphocytes. The intracellular domain (ICD) of ADAM10 associates with the HIV-1 pre-integration complex (PIC) in the cytoplasm and immunoprecipitates and co-localizes with HIV-1 integrase, a key component of PIC. Taken together, our data support a model whereby ADAM15/γ-secretase processing of ADAM10 releases the ICD, which then incorporates into HIV-1 PIC to facilitate nuclear trafficking. Thus, these studies suggest ADAM10 as a novel therapeutic target for inhibiting HIV-1 prior to nuclear entry.

Indexed as

Active Transport, Cell NucleusHost-Pathogen InteractionsVirus IntegrationADAM10 ProteinADAM ProteinsAmyloid Precursor Protein SecretasesCells, CulturedDNA, ViralHIV-1HumansImmunoprecipitationMacromolecular SubstancesMembrane ProteinsProtein BindingProtein Structure, TertiaryViral ProteinsADAM10 ProteinADAM10 protein, humanADAM ProteinsAmyloid Precursor Protein SecretasesDNA, ViralMacromolecular SubstancesMembrane ProteinsViral ProteinsADAM10ADAM15CD4(+) T lymphocytesHIV-1 integraseHIV-1 pre-integration complex (PIC)HIV-1 replicationMacrophagesγ-Secretase

Identifiers

PMID24725932
PMCPMC4018752
OpenAlexW1992780583

What OpenQuestion holds

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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.