Evidence map›Paper›PMID 35005938›Full record

ArticleACS applied bio materials2021

Controlled Modular Multivalent Presentation of the CD40 Ligand on P22 Virus-like Particles Leads to Tunable Amplification of CD40 Signaling.

Cheri Peyton Goodall, Benjamin Schwarz, Ekaterina Selivanovitch, John Avera, Joseph Wang, Heini Miettinen, Trevor Douglas

Open access · greenAbstract read
In one paragraph

Article in ACS applied bio materials, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Chemical reviews · 2026
    Review
  2. Templated trimerization of the phage L decoration protein on capsids.Protein science : a publication of the Protein Society · 2025
    Article
  3. Templated trimerization of the phage L decoration protein on capsids.bioRxiv : the preprint server for biology · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. 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

7 authors at 4 institutions in 1 country.

Cheri Peyton GoodallDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, Indiana 47405, United States.ORCID 0000-0003-2044-367X
Benjamin SchwarzLaboratory of Bacteriology, National Institute of Allergy and Infectious Diseases, 903 South 4th Street, Hamilton, Montana 59840, United States.
Ekaterina SelivanovitchDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, Indiana 47405, United States.
John AveraWalden Biosciences, One Kendall Square, Suite 7102, Cambridge, Massachusetts 02139, United States.
Joseph WangDepartment of Microbiology and Immunology, The Pennsylvania State University College of Medicine, 700 HMC Crescent Road, Hershey, Pennsylvania 17033, United States.ORCID 0000-0001-6580-3531
Heini MiettinenDepartment of Microbiology and Immunology, Montana State University, P.O. Box 173520, Bozeman, Montana 59717, United States.ORCID 0000-0001-6249-8615
Trevor DouglasDepartment of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, Indiana 47405, United States.ORCID 0000-0002-7882-2704
Indiana University Bloomington · USMontana State University · USNational Institute of Allergy and Infectious Diseases · USPennsylvania State University · US

Funding

Graduate Program in Quantitative and Chemical Biology at Indiana University BloomT32GM109825 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 2014 to 2018
$926k
NIGMS NIH HHS T32 GM109825
6 · The paper itself

Abstract

Ligands of the tumor necrosis factor superfamily (TNFSF) are appealing targets for immunotherapy research due to their integral involvement in stimulation or restriction of immune responses. TNFSF-targeted therapies are currently being developed to combat immunologically based diseases and cancer. A crucial determinant of effective TNFSF receptor binding and signaling is the trimeric quaternary structure of the ligand. Additionally, ligand multivalency is essential to propagate strong signaling in effector cells. Thus, designing a synthetic platform to display trimeric TNFSF ligands in a multivalent manner is necessary to further the understanding of ligand-receptor interactions. Viral nanocages have architectures that are amenable to genetic and chemical modifications of both their interior and exterior surfaces. Notably, the exterior surface of virus-like particles can be utilized as a platform for the modular multivalent presentation of target proteins. In this study, we build on previous efforts exploring the bacteriophage P22 virus-like particle for the exterior multivalent modular display of a potent immune-stimulating TNFSF protein, CD40 ligand (CD40L). Using a cell-based reporter system, we quantify the effects of tunable avidity on CD40 signaling by CD40L displayed on the surface of P22 nanocages. Multivalent presentation of CD40L resulted in a 53.6-fold decrease of the half maximal effective concentration (EC

Indexed as

Bacteriophage P22CD40 LigandLigandsSignal TransductionTumor Necrosis Factor-alphaCD40 LigandLigandsTumor Necrosis Factor-alphabiomimeticsCD40CD40LmultivalencyP22signalingTNFSFVLP

Identifiers

PMID35005938
PMCPMC9136706
OpenAlexW3212392255

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.