Evidence map›Paper›PMID 11739697›Full record

ArticleJournal of virology2002

Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor.

David T Evans, Karl C Tillman, Ronald C Desrosiers

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  8. Article
  9. Review
  10. Article
  11. Mechanisms for Env glycoprotein acquisition by retroviruses.AIDS research and human retroviruses · 2011
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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.

David T EvansNew England Regional Primate Research Center, Harvard Medical School, Southborough, Massachusetts 01772-9102, USA.
Karl C Tillman
Ronald C Desrosiers
Harvard University · US

Funding

ZETA CHAIN OF T CELL RECEPTOR INTERACTS W/ NEF OF SIV &HIV2P51RR000168 · NCRR · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JOHNSON, R. PAUL · 1985 to 2011
$139.3M
MOLECULAR BASIS FOR STV PATHOGENICITYR37AI025328 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI DESROSIERS, RONALD C · 1996 to 2005
$2.5M
MOLECULAR BASIS FOR SIV PATHOGENICITYR01AI025328 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI DESROSIERS, RONALD C · 1987 to 2010
$2.0M
MOUSE MODELS OF CANCER, BONE DISEASE, AND LACTATIONK26RR000168 · NCRR · OHIO STATE UNIVERSITY · PI ROSOL, THOMAS J · 2000 to 2004
$547k
MUCOSAL TRANSMISSION OF SINGLE-CYCLE SIV RECOMBINANTSF32AI010464 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI EVANS, DAVID T · 2000 to 2002
$128k
NCRR NIH HHS K26 RR000168NCRR NIH HHS P51 RR000168NCRR NIH HHS RR00168NIAID NIH HHS AI10464-02NIAID NIH HHS AI25328NIAID NIH HHS F32 AI010464NIAID NIH HHS R01 AI025328NIAID NIH HHS R37 AI025328
6 · The paper itself

Abstract

Lentivirus envelope glycoproteins have unusually long cytoplasmic domains compared to those of other retroviruses. To identify cellular binding partners of the simian immunodeficiency virus (SIV) envelope transmembrane protein (gp41) cytoplasmic domain (CD), we performed a yeast two-hybrid screen of a phytohemagglutinin-activated human T-cell cDNA library with the SIV gp41 CD. The majority of positive clones (50 of 54) encoded the prenylated Rab acceptor (PRA1). PRA1 is a 21-kDa protein associated with Golgi membranes that binds to prenylated Rab proteins in their GTP-bound state. While the cellular function of PRA1 is presently unknown, this protein appears to participate in intracellular vesicular trafficking, based on its cellular localization and ability to bind multiple members of the Rab protein family. Mammalian two-hybrid assays confirmed the interaction between the SIV gp41 CD and PRA1. Furthermore, gp41 sequences important for PRA1 binding were mapped to a central leucine-rich, amphipathic alpha-helix in the SIV gp41 cytoplasmic tail. Although the human immunodeficiency virus (HIV-1) gp41 CD failed to interact with PRA1 in the yeast two-hybrid system, its interaction with PRA1 was significantly better than that of the SIV gp41 CD in mammalian two-hybrid assays. Interestingly, PRA1 also interacted with the Env CDs of HIV-2, bovine immunodeficiency virus, equine infectious anemia virus, and feline immunodeficiency virus. Thus, PRA1 associates with envelope glycoproteins from widely divergent lentiviruses.

Indexed as

Amino Acid SequenceCarrier ProteinsCell LineGTP-Binding ProteinsHumansLentivirusMembrane GlycoproteinsMembrane ProteinsMolecular Sequence DataProtein BindingRetroviridae ProteinsSimian Immunodeficiency VirusTwo-Hybrid System TechniquesVesicular Transport ProteinsViral Envelope ProteinsVirus ReplicationCarrier ProteinsGTP-Binding ProteinsMembrane GlycoproteinsMembrane ProteinsRABAC1 protein, humanRetroviridae ProteinsSIV envelope protein gp41Vesicular Transport ProteinsViral Envelope Proteins

Identifiers

PMID11739697
PMCPMC135700
OpenAlexW2101876289

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.