Evidence map›Paper›PMID 18076768›Full record

ArticleRetrovirology2007

Asn 362 in gp120 contributes to enhanced fusogenicity by CCR5-restricted HIV-1 envelope glycoprotein variants from patients with AIDS.

Jasminka Sterjovski, Melissa J Churchill, Anne Ellett, Lachlan R Gray, Michael J Roche, Rebecca L Dunfee, Damian F J Purcell, Nitin Saksena, Bin Wang, Secondo Sonza and 6 more

Open access · goldAbstract read
In one paragraph

Article in Retrovirology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

65 citing papers in PubMed, 91 citations in OpenAlex.

  1. Viral syncytia evolve to resist interferon.Nature communications · 2026
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5 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

16 authors at 6 institutions in 3 countries.

Jasminka SterjovskiMacfarlane Burnet Institute for Medical Research & Public Health, Melbourne, Victoria, Australia. Jasminka@burnet.edu.au
Melissa J Churchill
Anne Ellett
Lachlan R Gray
Michael J Roche
Rebecca L Dunfee
Damian F J Purcell
Nitin Saksena
Bin Wang
Secondo Sonza
Steven L Wesselingh
Ingrid Karlsson
Eva-Maria Fenyo
Dana Gabuzda
Anthony L Cunningham
Paul R Gorry
Burnet Institute · AUWestmead Institute · AUDana-Farber Cancer Institute · USLund University · SEMonash University · AUUniversity of Melbourne · AU

Funding

CHEMOKINE RECEPTORS IN HIV1 INFECTION OF THE CNSR01NS037277 · NINDS · DANA-FARBER CANCER INSTITUTE · PI GABUZDA, DANA H. · 1998 to 2006
$2.9M
Pathogenesis of Macrophage Tropic HIV-1R21AI054207 · NIAID · MACFARLANE BURNET INST FOR RES/PUB HLTH · PI GORRY, PAUL R · 2003 to 2004
$324k
NIAID NIH HHS AI054207NIAID NIH HHS R21 AI054207NINDS NIH HHS NS37277NINDS NIH HHS R01 NS037277
6 · The paper itself

Abstract

backgroundCCR5-restricted (R5) human immunodeficiency virus type 1 (HIV-1) variants cause CD4+ T-cell loss in the majority of individuals who progress to AIDS, but mechanisms underlying the pathogenicity of R5 strains are poorly understood. To better understand envelope glycoprotein (Env) determinants contributing to pathogenicity of R5 viruses, we characterized 37 full-length R5 Envs from cross-sectional and longitudinal R5 viruses isolated from blood of patients with asymptomatic infection or AIDS, referred to as pre-AIDS (PA) and AIDS (A) R5 Envs, respectively.

resultsCompared to PA-R5 Envs, A-R5 Envs had enhanced fusogenicity in quantitative cell-cell fusion assays, and reduced sensitivity to inhibition by the fusion inhibitor T-20. Sequence analysis identified the presence of Asn 362 (N362), a potential N-linked glycosylation site immediately N-terminal to CD4-binding site (CD4bs) residues in the C3 region of gp120, more frequently in A-R5 Envs than PA-R5 Envs. N362 was associated with enhanced fusogenicity, faster entry kinetics, and increased sensitivity of Env-pseudotyped reporter viruses to neutralization by the CD4bs-directed Env mAb IgG1b12. Mutagenesis studies showed N362 contributes to enhanced fusogenicity of most A-R5 Envs. Molecular models indicate N362 is located adjacent to the CD4 binding loop of gp120, and suggest N362 may enhance fusogenicity by promoting greater exposure of the CD4bs and/or stabilizing the CD4-bound Env structure.

conclusionEnhanced fusogenicity is a phenotype of the A-R5 Envs studied, which was associated with the presence of N362, enhanced HIV-1 entry kinetics and increased CD4bs exposure in gp120. N362 contributes to fusogenicity of R5 Envs in a strain dependent manner. Our studies suggest enhanced fusogenicity of A-R5 Envs may contribute to CD4+ T-cell loss in subjects who progress to AIDS whilst harbouring R5 HIV-1 variants. N362 may contribute to this effect in some individuals.

Indexed as

Acquired Immunodeficiency SyndromeAsparagineCD4 AntigensCell FusionCells, CulturedHIV-1HIV Envelope Protein gp120HumansLeukocytes, MononuclearModels, MolecularReceptors, CCR5VirulenceVirus AttachmentAsparagineCD4 AntigensHIV Envelope Protein gp120Receptors, CCR5

Identifiers

PMID18076768
PMCPMC2225424
OpenAlexW2152971024

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.