Evidence map›Paper›PMID 29806004›Full record

ArticleACS central science2018

Multivalent Antigen Presentation Enhances the Immunogenicity of a Synthetic Three-Component HIV-1 V3 Glycopeptide Vaccine.

Hui Cai, Roushu Zhang, Jared Orwenyo, John Giddens, Qiang Yang, Celia C LaBranche, David C Montefiori, Lai-Xi Wang

Abstract read
In one paragraph

Article in ACS central science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Review
  2. ACS central science · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Peptides for Vaccine Development.ACS applied bio materials · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Emerging microbes & infections · 2020
    Article
  12. Article
  13. Review
  14. Article
  15. Chemoenzymatic Synthesis of HIV-1 Glycopeptide Antigens.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  16. Review
  17. Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019
    Review
  18. Article
  19. Article
  20. Review
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

8 authors.

Hui CaiDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
Roushu ZhangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
Jared OrwenyoDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
John GiddensDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
Qiang YangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
Celia C LaBrancheDepartment of Surgery, Duke University Medical Center, Durham, North Carolina 27705, United States.
David C MontefioriDepartment of Surgery, Duke University Medical Center, Durham, North Carolina 27705, United States.
Lai-Xi WangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.

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

HIV-1 envelope glycoproteins gp120 and gp41 are presented on the virus surface as a trimer of heterodimer and are the targets of broadly neutralizing antibodies (bNAbs). We describe here the synthesis and preliminary immunological evaluation of a three-component trivalent HIV-1 V3 glycopeptide immunogen aiming to raise glycopeptide epitope-specific antibodies. Click chemistry confers efficient synthesis of the lipopeptide-glycopeptide conjugate that carries three copies of HIV-1 JR-FL gp120 V3 glycopeptide with a high-mannose glycan at the N332 glycosylation site. We found that the multivalent presentation substantially enhanced the immunogenicity of the V3 glycopeptide. The antisera induced by the three-component multivalent glycopeptide immunogen exhibited stronger binding to heterologous HIV-1 gp120s and the trimeric gp140s than that from the monovalent glycopeptide immunogen. The antisera generated from this preliminary rabbit immunization did not show virus neutralization activity, probably due to the lack of somatic maturation. The ability to elicit substantial glycopeptide epitope-specific antibodies by the three-component trivalent glycopeptide immunogen suggests that it could serve as a valuable vaccine component in combination with other vaccine candidates for further immunization studies.

Identifiers

PMID29806004
PMCPMC5968512

What OpenQuestion holds

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Registered trials

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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.