Evidence map›Paper›PMID 22830650›Full record

ArticleBiomacromolecules2012

Engineered mutations change the structure and stability of a virus-like particle.

Jason D Fiedler, Cody Higginson, Marisa L Hovlid, Alexander A Kislukhin, Alexandra Castillejos, Florian Manzenrieder, Melody G Campbell, Neil R Voss, Clinton S Potter, Bridget Carragher and 1 more

Abstract read
In one paragraph

Article in Biomacromolecules, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

41 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  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. Review
  9. Cell binding tropism of rat hepatitis E virus is a pivotal determinant of its zoonotic transmission to humans.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Decoration ofInfection and immunity · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Virus-like particle vaccinology, from bench to bedside.Cellular & molecular immunology · 2022
    Review
  19. Virus-like Particles: Fundamentals and Biomedical Applications.International journal of molecular sciences · 2022
    Review
  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

11 authors at 1 institution in 1 country.

Jason D FiedlerDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.
Cody Higginson
Marisa L Hovlid
Alexander A Kislukhin
Alexandra Castillejos
Florian Manzenrieder
Melody G Campbell
Neil R Voss
Clinton S Potter
Bridget Carragher
M G Finn
Scripps Research Institute · 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
WORKSHOPS AND TRAININGP41RR017573 · NCRR · SCRIPPS RESEARCH INSTITUTE, THE · PI CARRAGHER, BRIDGET OLIVIA · 2002 to 2011
$14.2M
Virus-Like Particle Based Antigen Display as Multi-component Anticancer VaccinesR01CA149451 · NCI · MICHIGAN STATE UNIVERSITY · PI HUANG, XUEFEI · 2011 to 2015
$2.4M
Predoctoral Training Program in Molecular EvolutionT32GM080209 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI FINN, M.G. · 2009 to 2011
$461k
NCI NIH HHS CA149451NCI NIH HHS R01 CA149451NCRR NIH HHS P41 RR017573NCRR NIH HHS RR017573NIGMS NIH HHS GM103310NIGMS NIH HHS P41 GM103310NIGMS NIH HHS T32 GM080209NIGMS NIH HHS T32-GM080209
6 · The paper itself

Abstract

The single-coat protein (CP) of bacteriophage Qβ self-assembles into T = 3 icosahedral virus-like particles (VLPs), of interest for a wide range of applications. These VLPs are very stable, but identification of the specific molecular determinants of this stability is lacking. To investigate these determinants along with manipulations that confer more capabilities to our VLP material, we manipulated the CP primary structure to test the importance of various putative stabilizing interactions. Optimization of a procedure to incorporate fused CP subunits allowed for good control over the average number of covalent dimers in each VLP. We confirmed that the disulfide linkages are the most important stabilizing elements for the capsid and that acidic conditions significantly enhance the resistance of VLPs to thermal degradation. Interdimer interactions were found to be less important for VLP assembly than intradimer interactions. Finally, a single point mutation in the CP resulted in a population of smaller VLPs in three distinct structural forms.

Indexed as

Amino Acid SubstitutionAllolevivirusAmino Acid MotifsCapsidCapsid ProteinsEscherichia coliHydrogen BondingHydrophobic and Hydrophilic InteractionsInverted Repeat SequencesLightModels, MolecularPoint MutationProtein EngineeringProtein Interaction Domains and MotifsProtein MultimerizationProtein StabilityCapsid ProteinsRNA, Viral

Identifiers

PMID22830650
PMCPMC3432585
OpenAlexW2079670884

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.