Evidence map›Paper›PMID 20686044›Full record

ArticleJournal of virology2010

Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16.

Katie J Doores, Dennis R Burton

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 178 papers.

0numbers the graph read from it
0cells of the map it votes in
178citing papers in PubMed
8.7field-weighted citation impact, top 1% 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

178 citing papers in PubMed, 238 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Trial
  4. Trial
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

118 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

2 authors at 1 institution in 1 country.

Katie J DooresDepartment of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
Dennis R Burton
Scripps Research Institute · US

Funding

HUMAN ANTIBODIES TO HIV-1 BY REPERTOIRE CLONINGR01AI033292 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BURTON, DENNIS R. · 1992 to 2013
$5.9M
HUMAN ANTIBODIES TO HIV-1 BY REPERTOIRE CLONINGR37AI033292 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI BURTON, DENNIS R. · 1995 to 2004
$2.4M
NIAID NIH HHS AI33292NIAID NIH HHS R01 AI033292NIAID NIH HHS R37 AI033292
6 · The paper itself

Abstract

The HIV-1-specific antibodies PG9 and PG16 show marked cross-isolate neutralization breadth and potency. Antibody neutralization has been shown to be dependent on the presence of N-linked glycosylation at position 160 in gp120. We show here that (i) the loss of several key glycosylation sites in the V1, V2, and V3 loops; (ii) the generation of pseudoviruses in the presence of various glycosidase inhibitors; and (iii) the growth of pseudoviruses in a mutant cell line (GnT1(-/-)) that alters envelope glycosylation patterns all have significant effects on the sensitivity of virus to neutralization by PG9 and PG16. However, the interaction of antibody is not inhibited by sugar monosaccharides corresponding to those found in glycans on the HIV surface. We show that some of the glycosylation effects described are isolate dependent and others are universal and can be used as diagnostic for the presence of PG9 and PG16-like antibodies in the sera of HIV-1-infected patients. The results suggest that PG9 and PG16 recognize a conformational epitope that is dependent on glycosylation at specific variable loop N-linked sites. This information may be valuable for the design of immunogens to elicit PG9 and PG16-like antibodies, as well as constructs for cocrystallization studies.

Indexed as

Amino Acid SubstitutionAntibodies, NeutralizingBinding, CompetitiveBinding SitesCell LineEpitopesGlycosylationHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansMonosaccharidesMutagenesis, Site-DirectedPeptide FragmentsPolysaccharidesProtein ConformationAntibodies, NeutralizingEpitopesHIV AntibodiesHIV Envelope Protein gp120MonosaccharidesPeptide FragmentsPolysaccharidesRecombinant ProteinsSwainsonine

Identifiers

PMID20686044
PMCPMC2950566
OpenAlexW2083627780

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.