Evidence map›Paper›PMID 10864659›Full record

ArticleJournal of virology2000

Soluble receptor-induced retroviral infection of receptor-deficient cells.

R Damico, P Bates

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Retroviral host range extension is coupled with Env-activating mutations resulting in receptor-independent entry.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

2 authors at 1 institution in 1 country.

R DamicoDepartment of Microbiology, Graduate Program in Cellular and Molecular Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6076, USA.
P Bates
University of Pennsylvania · US

Funding

TRAINING PROGRAM IN CELL AND MOLECULAR BIOLOGYT32GM007229 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BARTOLOMEI, MARISA S. · 1985 to 2023
$14.0M
FUNCTIONAL ANALYSIS OF RSV ENVELOPE GLYCOPROTEINR01CA076256 · NCI · UNIVERSITY OF PENNSYLVANIA · PI BATES, PAUL F · 1998 to 2002
$787k
CELLULAR RECEPTOR FOR ROUS SARCOMA VIRUSR29CA063531 · NCI · UNIVERSITY OF PENNSYLVANIA · PI BATES, PAUL F · 1994 to 1998
–
NCI NIH HHS CA63531NCI NIH HHS CA76256NCI NIH HHS R01 CA076256NIGMS NIH HHS T32 GM007229NIGMS NIH HHS T32 GM07229
6 · The paper itself

Abstract

Current models of retroviral entry hypothesize that interactions between the host cell receptor(s) and viral envelope protein induce structural changes in the envelope protein that convert it to an active conformation, allowing it to mediate fusion with the membrane. Recent evidence supporting this hypothesis is the demonstration that Tva, the receptor for subgroup A avian sarcoma and leukosis virus (ASLV-A), induces conformational changes in the viral envelope protein. These changes include conversion of the envelope protein to an active, membrane-binding state likely representing a fusogenic conformation. To determine whether binding of the soluble Tva (sTva) receptor was sufficient to activate fully the fusogenic potential of the ASLV-A envelope protein, we have evaluated the ability of ASLV-A to infect receptor-deficient cell lines in the presence of sTva. Soluble receptor efficiently mediated infection of cells devoid of endogenous Tva in a dose-dependent manner, and this infection was dependent absolutely on the addition of sTva. The infectivity of the virus was enhanced dramatically in the presence of the polycationic polymer Polybrene or when centrifugal forces were applied during inoculation, resulting in viral titers comparable to those achieved on cells expressing endogenous receptor. sTva functioned to mediate infection at low concentrations, approaching the estimated binding constant of the receptor and viral envelope protein. These results demonstrate that receptor binding can activate the ASLV-A envelope protein and convert it to a fusogenic conformation competent to mediate the fusion of the viral and cellular membranes.

Indexed as

AlpharetrovirusAvian ProteinsCell LineGene Products, envHexadimethrine BromideHumansProtein BindingReceptors, VirusSolubilityAvian ProteinsGene Products, envHexadimethrine BromideReceptors, VirusTva receptor

Identifiers

PMID10864659
PMCPMC112155
OpenAlexW2170406054

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.