Evidence map›Paper›PMID 32234486›Full record

ArticleCell reports2020

Structure-Based Design of Prefusion-Stabilized Filovirus Glycoprotein Trimers.

Lucy Rutten, Morgan S A Gilman, Sven Blokland, Jarek Juraszek, Jason S McLellan, Johannes P M Langedijk

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
1.0field-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

56 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Structure-based design of a soluble human cytomegalovirus glycoprotein B antigen stabilized in a prefusion-like conformation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Strategies of rational and structure-driven vaccine design for Arenaviruses.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2024
    Review
  20. 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

6 authors at 2 institutions in 2 countries.

Lucy RuttenJanssen Vaccines & Prevention, Archimedesweg 4-6, Leiden 2333 CN, the Netherlands.
Morgan S A GilmanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA.
Sven BloklandJanssen Vaccines & Prevention, Archimedesweg 4-6, Leiden 2333 CN, the Netherlands.
Jarek JuraszekJanssen Vaccines & Prevention, Archimedesweg 4-6, Leiden 2333 CN, the Netherlands.
Jason S McLellanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: jmclellan@austin.utexas.edu.
Johannes P M LangedijkJanssen Vaccines & Prevention, Archimedesweg 4-6, Leiden 2333 CN, the Netherlands. Electronic address: hlangedi@its.jnj.com.
Janssen (Netherlands) · NLThe University of Texas at Austin · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ebola virus causes severe hemorrhagic fever, often leading to death in humans. The trimeric fusion glycoprotein (GP) is the sole target for neutralizing antibodies and is the major focus of vaccine development. Soluble GP ectodomains are unstable and mostly monomeric when not fused to a heterologous trimerization domain. Here, we report structure-based designs of Ebola and Marburg GP trimers based on a stabilizing mutation in the hinge loop in refolding region 1 and substitution of a partially buried charge at the interface of the GP1 and GP2 subunits. The combined substitutions (T577P and K588F) substantially increased trimer expression for Ebola GP proteins. We determined the crystal structure of stabilized GP from the Makona Zaire ebolavirus strain without a trimerization domain or complexed ligand. The structure reveals that the stabilized GP adopts the same trimeric prefusion conformation, provides insight into triggering of GP conformational changes, and should inform future filovirus vaccine development.

Indexed as

Protein MultimerizationAmino Acid SubstitutionCell LineCrystallography, X-RayEbolavirusFiloviridaeGlycoproteinsHumansMarburgvirusModels, MolecularMutationPerfusionProtein DomainsProtein StabilityStructure-Activity RelationshipGlycoproteinscrystalEbolafilovirusglycoproteininstabilityMarburgprefusion trimersize-exclusion chromatographystabilizing substitutionsX-ray structure

Identifiers

PMID32234486
PMCPMC7118701
OpenAlexW3014406922

What OpenQuestion holds

Textmetadata
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.