Evidence map›Paper›PMID 20434554›Full record

ArticleVaccine2010

Immunogenic display of diverse peptides, including a broadly cross-type neutralizing human papillomavirus L2 epitope, on virus-like particles of the RNA bacteriophage PP7.

Jerri do Carmo Caldeira, Alexander Medford, Rhonda C Kines, Christopher A Lino, John T Schiller, Bryce Chackerian, David S Peabody

Abstract read
In one paragraph

Article in Vaccine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
9.9field-weighted citation impact, top 2% 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

62 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Bacteriophage Virus-Like Particles: Platforms for Vaccine Design.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. RNA Phage VLP-Based Vaccine Platforms.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  16. Article
  17. Review
  18. Article
  19. Vaccination Strategies for the Control and Treatment of HPV Infection and HPV-Associated Cancer.Recent results in cancer research. Fortschritte der Krebsforschung. Progres dans les recherches sur le cancer · 2021
    Article
  20. Review

2 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

7 authors at 2 institutions in 1 country.

Jerri do Carmo CaldeiraDepartment of Molecular Genetics and Microbiology, University of New Mexico School of Medicine, Albuquerque, NM 87131, USA.
Alexander Medford
Rhonda C Kines
Christopher A Lino
John T Schiller
Bryce Chackerian
David S Peabody
University of New Mexico · USNational Cancer Institute · US

Funding

Understanding Papillomavirus Virion Proteins and VaccinesZIABC009052 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHILLER, JOHN T. · 2009 to 2025
$38.4M
Web enhanced adoption of HPV vaccine in minority communitiesU19AI084081 · NIAID · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI STIDLEY, CHRISTINE A. · 2009 to 2013
$13.4M
RNA-BINDING SITE OF A TRANSLATIONAL REPRESSORR01GM042901 · NIGMS · UNIVERSITY OF NEW MEXICO · PI PEABODY, DAVID S. · 1991 to 2011
$2.7M
NIAID NIH HHS U19 AI084081NIGMS NIH HHS R01 GM042901
6 · The paper itself

Abstract

The immunogenicity of an antigen can be dramatically increased by displaying it in a dense, multivalent context, such as on the surface of a virus or virus-like particle (VLP). Here we describe a highly versatile VLP platform for peptide display based on VLPs of the RNA bacteriophage PP7. We show that this platform can be used for the engineered display of specific peptide sequences as well as for the construction of random peptide libraries. Peptides representing the FLAG epitope, the V3 loop of HIV gp120, and a broadly cross-type neutralizing epitope from L2, the minor capsid protein of Human Papillomavirus type 16 (HPV16), were inserted into an exposed surface loop of a form of PP7 coat protein in which the two identical polypeptides of coat were fused together to form a single-chain dimer. The recombinant proteins assembled into VLPs, displayed these peptides on their surfaces, and induced high-titer antibody responses. The single-chain dimer was also highly tolerant of random 6-, 8-, and 10-amino acid insertions. PP7 VLPs displaying the HPV16 L2 epitope generated robust anti-HPV16 L2 serum antibodies after intramuscular injection that protected mice from genital infection with HPV16 pseudovirus as well as a heterologous HPV pseudovirus type, HPV45. Thus, PP7 VLPs are well-suited for the display of a wide diversity of peptides in a highly immunogenic format.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCapsid ProteinsEpitopesFemaleMiceMolecular Sequence DataOncogene Proteins, ViralPapillomaviridaePeptide LibraryPeptidesRNA PhagesSequence AlignmentCapsid ProteinsEpitopesL2 protein, Human papillomavirus type 16Oncogene Proteins, ViralPeptide LibraryPeptides

Identifiers

PMID20434554
PMCPMC2881612
OpenAlexW2090347597

What OpenQuestion holds

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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.