Evidence map›Paper›PMID 12719582›Full record

ArticleJournal of virology2003

Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine design.

Ralph Pantophlet, Ian A Wilson, Dennis R Burton

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

75 citing papers in PubMed, 130 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Design of universal Ebola virus vaccine candidates via immunofocusing.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Design of universal Ebola virus vaccine candidatesbioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
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  17. Protect, modify, deprotect (PMD): A strategy for creating vaccines to elicit antibodies targeting a specific epitope.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Article
  20. Article

15 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

3 authors at 1 institution in 1 country.

Ralph PantophletDepartment of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.
Ian A Wilson
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
X-ray structures of HIV-1 neutralizing sitesR01GM046192 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 1991 to 2008
$3.7M
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 AI033292NIGMS NIH HHS GM46192NIGMS NIH HHS R01 GM046192
6 · The paper itself

Abstract

The ability to induce broadly neutralizing antibodies should be a key component of any forthcoming vaccine against human immunodeficiency virus type 1. One potential vaccine candidate, monomeric gp120, has generally failed to elicit such antibodies. We postulated that gp120 might be a better immunogen if it could be engineered to preferentially bind known broadly neutralizing antibodies. In a first study, we found that four alanine substitutions on the perimeter of the so-called Phe-43 cavity of gp120 could reduce binding of weakly neutralizing CD4-binding site antibodies (R. Pantophlet, E. O. Saphire, P. Poignard, P. W. H. I. Parren, I. A. Wilson, and D. R. Burton, J. Virol. 77:642-658, 2003), while slightly enhancing binding of the potent, broadly neutralizing antibody b12. In the present study, we sought to reduce or abolish the binding of a wider range of nonneutralizing antibodies, by incorporating extra N-glycosylation motifs at select positions into the hypervariable loops and the gp120 core. A hyperglycosylated mutant containing seven extra glycosylation sequons (consensus sequences) and the four alanine substitutions described above did not bind an extensive panel of nonneutralizing and weakly neutralizing antibodies, including a polyclonal immunoglobulin preparation (HIVIG) of low neutralizing potency. Binding of b12, at lowered affinity, and of four antibodies to the C1 and C5 regions was maintained. Removal of N- and C-terminal residues in the C1 and C5 regions, respectively, reduced or abolished binding of the four antibodies, but this also adversely affected b12 binding. The hyperglycosylated mutant and its analogues described here are novel antigens that may provide a new approach to eliciting antibodies with b12-like neutralizing properties.

Indexed as

AIDS VaccinesDrug DesignHIV Envelope Protein gp120MutationAmino Acid SequenceAntibodies, MonoclonalCell LineGlycosylationHIV-1HIV AntibodiesHIV AntigensHumansModels, MolecularMolecular Sequence DataNeutralization TestsPolysaccharidesAIDS VaccinesAntibodies, MonoclonalHIV AntibodiesHIV AntigensHIV Envelope Protein gp120Polysaccharides

Identifiers

PMID12719582
PMCPMC154011
OpenAlexW2155429177

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.