Evidence map›Paper›PMID 30912918›Full record

ArticleACS nano2019

Engineering the PP7 Virus Capsid as a Peptide Display Platform.

Liangjun Zhao, Mykhailo Kopylov, Clinton S Potter, Bridget Carragher, M G Finn

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.8field-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

38 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Chemical reviews · 2026
    Review
  6. Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Genetically EncodedACS synthetic biology · 2025
    Article
  11. Review
  12. Article
  13. Multi-species cryoEM calibration and workflow verification standard.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  14. Article
  15. Multi-species cryoEM calibration and workflow verification standard.bioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Glycan-costumed virus-like particles promote type 1 anti-tumor immunity.bioRxiv : the preprint server for biology · 2024
    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

5 authors at 2 institutions in 1 country.

Mykhailo KopylovNational Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center , 89 Convent Avenue , New York , New York 10027 , United States.
Clinton S PotterNational Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center , 89 Convent Avenue , New York , New York 10027 , United States.
Bridget CarragherNational Resource for Automated Molecular Microscopy, Simons Electron Microscopy Center, New York Structural Biology Center , 89 Convent Avenue , New York , New York 10027 , United States.
New York Structural Biology Center · USGeorgia Institute of Technology · US

Funding

TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Acquisition of Detector for JEOL 3200 FSC Electron MicroscopeS10OD019994 · OD · NEW YORK STRUCTURAL BIOLOGY CENTER · PI CARRAGHER, BRIDGET OLIVIA · 2015 to 2015
$600k
NIGMS NIH HHS P41 GM103310NIH HHS S10 OD019994
6 · The paper itself

Abstract

As self-assembling polyvalent nanoscale structures that can tolerate substantial genetic and chemical modification, virus-like particles are useful in a variety of fields. Here we describe the genetic modification and structural characterization of the Leviviridae PP7 capsid protein as a platform for the presentation of functional polypeptides. This particle was shown to tolerate the display of sequences from 1 kDa (a cell penetrating peptide) to 14 kDa (the Fc-binding double Z-domain) on its exterior surface as C-terminal genetic fusions to the coat protein. In addition, a dimeric construct allowed the presentation of exogenous loops between capsid monomers and the simultaneous presentation of two different peptides at different positions on the icosahedral structure. The PP7 particle is thereby significantly more tolerant of these types of polypeptide additions than Qβ and MS2, the other Leviviridae-derived VLPs in common use.

Indexed as

Peptide LibraryAmino Acid SequenceCapsidCapsid ProteinsLeviviridaeModels, MolecularPeptidesProtein EngineeringCapsid ProteinsPeptide LibraryPeptidescryo-electron microscopypackaged enzymespeptide displayprotein nanoparticlesvirus-like particles

Identifiers

PMID30912918
PMCPMC6991139
OpenAlexW2923293346

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.