Evidence map›Paper›PMID 32407684›Full record

ArticleBiophysical journal2020

Membrane Association Transforms an Inert Anti-TCRβ Fab' Ligand into a Potent T Cell Receptor Agonist.

Jenny J Lin, Geoff P O'Donoghue, Kiera B Wilhelm, Michael P Coyle, Shalini T Low-Nam, Nicole C Fay, Katherine N Alfieri, Jay T Groves

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Differential roles of kinetic on- and off-rates in T-cell receptor signal integration revealed with a modified Fab'-DNA ligand.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  8. Trapping or slowing the diffusion of T cell receptors at close contacts initiates T cell signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  13. Review
  14. Article
  15. Clustering of the ζ-Chain Can Initiate T Cell Receptor Signaling.International journal of molecular sciences · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Jenny J LinDepartment of Chemistry, University of California, Berkeley, Berkeley, California.
Geoff P O'DonoghueDepartment of Chemistry, University of California, Berkeley, Berkeley, California. Electronic address: geoff.odonoghue@gmail.com.
Kiera B WilhelmDepartment of Chemistry, University of California, Berkeley, Berkeley, California.
Michael P CoyleDepartment of Chemistry, University of California, Berkeley, Berkeley, California. Electronic address: coylem6@gmail.com.
Shalini T Low-NamDepartment of Chemistry, University of California, Berkeley, Berkeley, California.
Nicole C FayDepartment of Molecular and Cellular Biology, University of California, Berkeley, Berkeley, California.
Katherine N AlfieriDepartment of Chemistry, University of California, Berkeley, Berkeley, California.
Jay T GrovesDepartment of Chemistry, University of California, Berkeley, Berkeley, California. Electronic address: jtgroves@lbl.gov.
University of California, Berkeley · US

Funding

Understand the metabolic fitness of naïve T cellsP01AI091580 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JEROEN ROOSE · 2011 to 2026
$31.1M
NIAID NIH HHS P01 AI091580
6 · The paper itself

Abstract

The natural peptide-major histocompatibility complex (pMHC) ligand for T cell receptors (TCRs) is inactive from solution yet capable of activating T cells at single-molecule levels when membrane-associated. This distinctive feature stems from the mechanism of TCR activation, which is thought to involve steric phosphatase exclusion as well as direct mechanical forces. It is possible to defeat this mechanism and activate T cells with solution ligands by cross-linking pMHC or using multivalent antibodies to TCR. However, these widely used strategies activate TCRs through a nonphysiological mechanism and can produce different activation profiles than natural, monovalent, membrane-associated pMHC. Here, we introduce a strictly monovalent anti-TCRβ H57 Fab' ligand that, when coupled to a supported lipid bilayer via DNA complementation, triggers TCRs and activates nuclear translocation of the transcription factor nuclear factor of activated T cells (NFAT) with a similar potency to pMHC in primary murine T cells. Importantly, like monovalent pMHC and unlike bivalent antibodies, monovalent Fab'-DNA triggers TCRs only when physically coupled to the membrane, and only around 100 individual Fab':TCR interactions are necessary to stimulate early T cell activation.

Indexed as

Lymphocyte ActivationReceptors, Antigen, T-CellAnimalsLigandsMajor Histocompatibility ComplexMiceT-LymphocytesLigandsReceptors, Antigen, T-Cell

Identifiers

PMID32407684
PMCPMC7300389
OpenAlexW3019673336

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.