Evidence map›Paper›PMID 9420225›Full record

ArticleJournal of virology1998

Amino-terminal substitutions in the CCR5 coreceptor impair gp120 binding and human immunodeficiency virus type 1 entry.

T Dragic, A Trkola, S W Lin, K A Nagashima, F Kajumo, L Zhao, W C Olson, L Wu, C R Mackay, G P Allaway and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
6.0field-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

91 citing papers in PubMed, 216 citations in OpenAlex.

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31 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

13 authors at 5 institutions in 1 country.

T DragicAaron Diamond AIDS Research Center, The Rockefeller University, New York, New York 10016, USA. tdragic@adarc.org
A Trkola
S W Lin
K A Nagashima
F Kajumo
L Zhao
W C Olson
L Wu
C R Mackay
G P Allaway
T P Sakmar
J P Moore
P J Maddon
Progenics Pharmaceuticals (United States) · USAaron Diamond AIDS Research Center · USHoward Hughes Medical Institute · USKalVista Pharmaceuticals (United States) · USRockefeller University · US

Funding

NIAID NIH HHS AI414420
6 · The paper itself

Abstract

The CC-chemokine receptor CCR5 is required for the efficient fusion of macrophage (M)-tropic human immunodeficiency virus type 1 (HIV-1) strains with the plasma membrane of CD4+ cells and interacts directly with the viral surface glycoprotein gp120. Although receptor chimera studies have provided useful information, the domains of CCR5 that function for HIV-1 entry, including the site of gp120 interaction, have not been unambiguously identified. Here, we use site-directed, alanine-scanning mutagenesis of CCR5 to show that substitutions of the negatively charged aspartic acid residues at positions 2 and 11 (D2A and D11A) and a glutamic acid residue at position 18 (E18A), individually or in combination, impair or abolish CCR5-mediated HIV-1 entry for the ADA and JR-FL M-tropic strains and the DH123 dual-tropic strain. These mutations also impair Env-mediated membrane fusion and the gp120-CCR5 interaction. Of these three residues, only D11 is necessary for CC-chemokine-mediated inhibition of HIV-1 entry, which is, however, also dependent on other extracellular CCR5 residues. Thus, the gp120 and CC-chemokine binding sites on CCR5 are only partially overlapping, and the former site requires negatively charged residues in the amino-terminal CCR5 domain.

Indexed as

Amino AcidsAmino Acid SequenceBinding SitesCCR5 Receptor AntagonistsCD4-Positive T-LymphocytesCell FusionCell LineChemokinesElectrochemistryHIV-1HIV Envelope Protein gp120HumansMacrophagesMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingAmino AcidsCCR5 Receptor AntagonistsChemokinesHIV Envelope Protein gp120Receptors, CCR5

Identifiers

PMID9420225
PMCPMC109374
OpenAlexW2132870230

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.