Evidence map›Paper›PMID 9636210›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

The ability of HIV type 1 to use CCR-3 as a coreceptor is controlled by envelope V1/V2 sequences acting in conjunction with a CCR-5 tropic V3 loop.

T M Ross, B R Cullen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Clinical significance of HIV-1 coreceptor usage.Journal of translational medicine · 2011
    Review
  5. Single-particle cryoelectron microscopy analysis reveals the HIV-1 spike as a tripod structure.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

2 authors at 2 institutions in 1 country.

T M RossDepartment of Genetics, Duke University Medical Center, Box 3025, Durham, NC 27710, USA.
B R Cullen
Duke University Hospital · USHoward Hughes Medical Institute · US

Funding

Ruth L. Kirschstein National Research Service Award (NRSA)- T32T32AI007392 · NIAID · DUKE UNIVERSITY · PI Amy Lynn Corneli, Guido Ferrari · 1990 to 2026
$9.8M
HIV-1 TROPISM AND CHEMOKINE RECEPTORSR01AI042538 · NIAID · DUKE UNIVERSITY · PI CULLEN, BRYAN R. · 1998 to 2002
$461k
NIAID NIH HHS 1R01AI42538NIAID NIH HHS 2T32AI07392NIAID NIH HHS T32 AI007392
6 · The paper itself

Abstract

Although infection by primary HIV type 1 (HIV-1) isolates normally requires the functional interaction of the viral envelope protein with both CD4 and the CCR-5 coreceptor, a subset of such isolates also are able to use the distinct CCR-3 receptor. By analyzing the ability of a series of wild-type and chimeric HIV-1 envelope proteins to mediate CCR-3-dependent infection, we have determined that CCR-3 tropism maps to the V1 and V2 variable region of envelope. Although substitution of the V1/V2 region of a CCR-3 tropic envelope into the context of a CCR-5 tropic envelope is both necessary and sufficient to confer CCR-3 tropism, this same substitution has no phenotypic effect when inserted into a CXCR-4 tropic HIV-1 envelope context. However, this latter chimera acquires both CCR-3 and CCR-5 tropism when a CCR-5 tropic V3 loop sequence also is introduced. These data demonstrate that the V1/2 region of envelope can, like the V3 loop region, encode a particular coreceptor requirement and suggest that a functional envelope:CCR-3 interaction may depend on the cooperative interaction of CCR-3 with both the V1/V2 and the V3 region of envelope.

Indexed as

HIV-1AnimalsCell FusionCloning, MolecularCOS CellsHIV Envelope Protein gp120Peptide FragmentsReceptors, CCR3Receptors, CCR5Receptors, ChemokineReceptors, HIVRecombinant Fusion ProteinsStructure-Activity RelationshipHIV Envelope Protein gp120HIV envelope protein gp120 (135-148)HIV envelope protein gp120 (305-321)Peptide FragmentsReceptors, CCR3Receptors, CCR5Receptors, ChemokineReceptors, HIVRecombinant Fusion Proteins

Identifiers

PMID9636210
PMCPMC22722
OpenAlexW2159899578

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.