Evidence map›Paper›PMID 28414420›Full record

ArticleACS chemical biology2017

Systematic Synthesis and Binding Study of HIV V3 Glycopeptides Reveal the Fine Epitopes of Several Broadly Neutralizing Antibodies.

Jared Orwenyo, Hui Cai, John Giddens, Mohammed N Amin, Christian Toonstra, Lai-Xi Wang

Abstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. ACS central science · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Peptides for Vaccine Development.ACS applied bio materials · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Chemoenzymatic Synthesis of HIV-1 Glycopeptide Antigens.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
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

6 authors at 1 institution in 1 country.

Jared OrwenyoDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland, United States.
Hui CaiDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland, United States.ORCID 0000-0002-5394-8167
John GiddensDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland, United States.
Mohammed N AminDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland, United States.
Christian ToonstraDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland, United States.
Lai-Xi WangDepartment of Chemistry and Biochemistry, University of Maryland , College Park, Maryland, United States.ORCID 0000-0003-4293-5819
University of Maryland, College Park · US

Funding

Synthetic HIV Vaccine Targeting Glycopeptide Neutralizing EpitopesR01AI113896 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2014 to 2018
$2.3M
NIAID NIH HHS R01 AI113896
6 · The paper itself

Abstract

A class of new glycan-reactive broadly neutralizing antibodies represented by PGT121, 10-1074, and PGT128 has recently been discovered that targets specific N-glycans and the peptide region around the V3 domain. However, the glycan specificity and fine epitopes of these bNAbs remain to be further defined. We report here a systematic chemoenzymatic synthesis of homogeneous V3 glycopeptides derived from the HIV-1 JR-FL strain carrying defined N-glycans at N332, N301, and N295 sites. Antibody binding studies revealed that both the nature and site of glycosylation in the context of the V3 domain were critical for high-affinity binding. It was found that antibody PGT128 exhibited specificity for high-mannose N-glycan with glycosylation site promiscuity, PGT121 showed binding specificity for glycopeptide carrying a sialylated N-glycan at N301 site, and 10-1074 was specific for glycopeptide carrying a high-mannose N-glycan at N332 site. The synthesis and binding studies permit a detailed assessment of the glycan specificity and the requirement of peptide in the context of antibody-antigen recognition. The identified glycopeptides can be used as potential templates for HIV vaccine design.

Indexed as

Antibodies, NeutralizingAntigen-Antibody ComplexBinding Sites, AntibodyEpitopesGlycopeptidesGlycosylationHIV Envelope Protein gp120HumansPeptide FragmentsPolysaccharidesAntibodies, NeutralizingAntigen-Antibody ComplexEpitopesGlycopeptidesHIV Envelope Protein gp120HIV envelope protein gp120 (305-321)Peptide FragmentsPolysaccharides

Identifiers

PMID28414420
PMCPMC5518477
OpenAlexW2607224847

What OpenQuestion holds

Textmetadata
LicenceTDM
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.