Evidence map›Paper›PMID 21501621›Full record

ArticleJournal of molecular biology2011

Peptide epitope identification by affinity selection on bacteriophage MS2 virus-like particles.

Bryce Chackerian, Jerri do Carmo Caldeira, Julianne Peabody, David S Peabody

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

35 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. RNA Phage VLP-Based Vaccine Platforms.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Evolving a Peptide: Library Platforms and Diversification Strategies.International journal of molecular sciences · 2019
    Review
  15. Review
  16. Article
  17. Article
  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

4 authors at 1 institution in 1 country.

Bryce ChackerianDepartment of Molecular Genetics and Microbiology, University of New Mexico School of Medicine, Albuquerque, NM 87131, USA. bchackerian@salud.unm.edu
Jerri do Carmo Caldeira
Julianne Peabody
David S Peabody
University of New Mexico · US

Funding

RNA-BINDING SITE OF A TRANSLATIONAL REPRESSORR01GM042901 · NIGMS · UNIVERSITY OF NEW MEXICO · PI PEABODY, DAVID S. · 1991 to 2011
$2.7M
A VLP-based platform for Vaccine DiscoveryR01AI083305 · NIAID · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI CHACKERIAN, BRYCE C · 2010 to 2013
$1.2M
NIAID NIH HHS R01 AI083305NIAID NIH HHS R01 AI08335NIGMS NIH HHS R01 GM042901
6 · The paper itself

Abstract

Filamentous phages are now the most widely used vehicles for phage display and provide efficient means for epitope identification. However, the peptides they display are not very immunogenic because they normally fail to present foreign epitopes at the very high densities required for efficient B-cell activation. Meanwhile, systems based on virus-like particles (VLPs) permit the engineered high-density display of specific epitopes but are incapable of peptide library display and affinity selection. We developed a new peptide display platform based on VLPs of the RNA bacteriophage MS2. It combines the high immunogenicity of MS2 VLPs with the affinity selection capabilities of other phage display systems. Here, we describe plasmid vectors that facilitate the construction of high-complexity random sequence peptide libraries on MS2 VLPs and that allow control of the stringency of affinity selection through the manipulation of display valency. We used the system to identify epitopes for several previously characterized monoclonal antibody targets and showed that the VLPs thus obtained elicit antibodies in mice whose activities mimic those of the selecting antibodies.

Indexed as

Affinity LabelsAmino Acid SequenceAnimalsAntibodies, MonoclonalAntigens, BacterialBacterial ToxinsCapsid ProteinsEnzyme-Linked Immunosorbent AssayEpitopesGenetic VectorsLevivirusMiceMice, Inbred BALB CMolecular Sequence DataPeptide FragmentsPeptide LibraryAffinity Labelsanthrax toxinAntibodies, MonoclonalAntigens, BacterialBacterial ToxinsCapsid ProteinsEpitopesPeptide FragmentsPeptide Library

Identifiers

PMID21501621
PMCPMC3095728
OpenAlexW1968134508

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.