Evidence map›Paper›PMID 15016849›Full record

ArticleJournal of virology2004

N-linked glycosylation of the V3 loop and the immunologically silent face of gp120 protects human immunodeficiency virus type 1 SF162 from neutralization by anti-gp120 and anti-gp41 antibodies.

Ruth A McCaffrey, Cheryl Saunders, Mike Hensel, Leonidas Stamatatos

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 6% 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

87 citing papers in PubMed, 1 synthesis or guideline pooled it, 150 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Stable, high yield expression of gp145 Env glycoprotein from HIV-1 in mammalian cells.Biologicals : journal of the International Association of Biological Standardization · 2021
    Article
  5. Article
  6. Impact of Protein Glycosylation on the Design of Viral Vaccines.Advances in biochemical engineering/biotechnology · 2021
    Review
  7. Article
  8. Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

27 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

4 authors at 2 institutions in 1 country.

Ruth A McCaffreySeattle Biomedical Research Institute. Department of Pathobiology, University of Washington, Seattle, Washington 98109, USA.
Cheryl Saunders
Mike Hensel
Leonidas Stamatatos
Center for Infectious Disease Research · USUniversity of Washington · US

Funding

VACCINE EFFICACY OF MODIFIED HIV ENVELOPESR01AI047708 · NIAID · SEATTLE BIOMEDICAL RESEARCH INSTITUTE · PI STAMATATOS, LEONIDAS · 2000 to 2010
$5.0M
Protection from SHIV-infection by CTL and AntibodiesR01AI051217 · NIAID · SEATTLE BIOMEDICAL RESEARCH INSTITUTE · PI STAMATATOS, LEONIDAS A · 2002 to 2006
$3.0M
Vaccine Efficacy of Modified HIV EnvelopesR56AI047708 · NIAID · SEATTLE BIOMEDICAL RESEARCH INSTITUTE · PI STAMATATOS, LEONIDAS · 2012 to 2012
$540k
NIAID NIH HHS AI47708NIAID NIH HHS AI51217NIAID NIH HHS R01 AI047708NIAID NIH HHS R01 AI051217NIAID NIH HHS R56 AI047708
6 · The paper itself

Abstract

We examined how asparagine-linked glycans within and adjacent to the V3 loop (C2 and C3 regions) and within the immunologically silent face (V4, C4, and V5 regions) of the human immunodeficiency virus (HIV) SF612 envelope affect the viral phenotype. Five of seven potential glycosylation sites are utilized when the virus is grown in human peripheral blood mononuclear cells, with the nonutilized sites lying within the V4 loop. Elimination of glycans within and adjacent to the V3 loop renders SF162 more susceptible to neutralization by polyclonal HIV(+)-positive and simian/human immunodeficiency virus-positive sera and by monoclonal antibodies (MAbs) recognizing the V3 loop, the CD4- and CCR5-binding sites, and the extracellular region of gp41. Importantly, our studies also indicate that glycans located within the immunologically silent face of gp120, specifically the C4 and V5 regions, also conferred on SF162 resistance to neutralization by anti-V3 loop, anti-CD4 binding site, and anti-gp41 MAbs but not by antibodies targeting the coreceptor binding site. We also observed that the amino acid composition of the V4 region contributes to the neutralization phenotype of SF162 by anti-V3 loop and anti-CD4 binding site MAbs. Collectively, our data support the proposal that the glycosylation and structure of the immunologically silent face of the HIV envelope plays an important role in defining the neutralization phenotype of HIV type 1.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalAsparagineCells, CulturedGlycosylationHIV-1HIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41HIV InfectionsHumansImmune SeraKineticsMolecular Sequence DataNeutralization TestsReceptors, HIVAntibodies, MonoclonalAsparagineHIV AntibodiesHIV Envelope Protein gp120HIV Envelope Protein gp41Immune SeraReceptors, HIV

Identifiers

PMID15016849
PMCPMC371088
OpenAlexW2165236706

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.