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Teniposide as a direct STING agonist

Candidate: toolkit item1 source documents5 linked claims
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Aliases

Teniposide

Extracted Explainers

What the tool is doing

Teniposide is presented here as a direct STING-binding small molecule that activates IFN-b2 signaling in a STING-dependent manner. The paper frames it as a repurposed STING agonist candidate.

Source 1DOIPubMed

Resources required

The reported characterization used high-throughput virtual screening, ITC against the STING cytosolic domain, a STING double mutant control, and docking plus molecular dynamics analyses. Functional testing also required assays of IFN-b2 pathway activation.

Source 1DOIPubMed

What problem it solves

It addresses the need to identify novel STING ligands for immune modulation. The source specifically suggests a cGAS-independent route to STING activation.

Source 1DOIPubMed

What it does not solve

The abstract does not show that teniposide solves questions of in vivo efficacy, selectivity, or clinical utility as a STING agonist. It also does not establish an experimentally solved binding structure.

Source 1DOIPubMed

Alternatives

The source positions teniposide against canonical cGAS-STING stimulation and mentions cGAS-dependent activation as the established route. The web summary also identifies cGAMP and other direct agonists as nearby comparators, but the abstract itself does not compare performance quantitatively.

Source 1DOIPubMed

Evidence Snippets

We employed high-throughput virtual screening to identify potential STING ligands and selected Teniposide... Direct binding of Teniposide to STING's cytosolic domain was confirmed... Teniposide activated the IFN-b2 signaling pathway in a STING-dependent manner.
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1binding mode modelsupports2025Source 1DOIPubMed

Computational analyses support a symmetrical binding mode in which two Teniposide molecules interact with STING.

Quoted textsource-backed
Computational analyses revealed a symmetrical binding mode involving two Teniposide molecules interacting with STING.
Claim 2binding specificity controlsupports2025Source 1DOIPubMed

A STING double mutant abolished Teniposide binding.

Quoted textsource-backed
the STING double mutant abolished binding
Claim 3direct bindingsupports2025Source 1DOIPubMed

Teniposide directly binds the STING cytosolic domain.

Quoted textsource-backed
Direct binding of Teniposide to STING's cytosolic domain was confirmed via isothermal titration calorimetry (ITC)
Claim 4mechanism independencesupports2025Source 1DOIPubMed

Teniposide-triggered STING signaling is independent of cGAS and IFI16.

Quoted textsource-backed
Teniposide activated the IFN-b2 signaling pathway in a STING-dependent manner, independent of dsDNA sensors cyclic GMP-AMP synthase (cGAS) and Interferon Gamma Inducible Protein 16 (IFI16).
Claim 5pathway activationsupports2025Source 1DOIPubMed

Teniposide activates the IFN-b2 signaling pathway in a STING-dependent manner.

Quoted textsource-backed
Teniposide activated the IFN-b2 signaling pathway in a STING-dependent manner