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TitleDevelopment of DARPin T cell engagers for specific targeting of tumor-associated HLA/peptide complexes.
Journal, issue, pagesiScience, Vol. 28, Issue 12, Page 113926, Year 2025
Publish dateDec 19, 2025
AuthorsNatalia Venetz-Arenas / Tim Schulte / Sandra Müller / Karin Wallden / Stefanie Fischer / Tom Resink / Nadir Kadri / Maria Paladino / Nicole Pina / Filip Radom / Denis Villemagne / Sandra Bruckmaier / Andreas Cornelius / Tanja Hospodarsch / Evren Alici / Hans-Gustaf Ljunggren / Benedict J Chambers / Xiao Han / Renhua Sun / Marta Carroni / Victor Levitsky / Tatyana Sandalova / Marcel Walser / Adnane Achour /
PubMed AbstractThe balance between affinity and specificity in T cell receptor (TCR)-dependent targeting of HLA-restricted tumor-associated antigens presents a significant challenge for immunotherapy development. T ...The balance between affinity and specificity in T cell receptor (TCR)-dependent targeting of HLA-restricted tumor-associated antigens presents a significant challenge for immunotherapy development. T cell engagers that circumvent these limitations are therefore of particular interest. We established a process to generate bispecific designed ankyrin repeat proteins (DARPins) that simultaneously target HLA-I/peptide complexes and CD3e. These high-affinity T cell engagers elicited CD8 T cell activation against tumor targets with strong peptide specificity, as confirmed by X-scanning mutagenesis and functional killing assays. A cryo-EM structure of the ternary DARPin/HLA-A∗0201/NY-ESO1 complex revealed a rigid, concave DARPin surface spanning the full length of the peptide-binding cleft, contacting both α-helices and the peptide. The present findings reveal promising immuno-oncotherapeutic approaches and demonstrate the feasibility of rapidly developing DARPins with high affinity and specificity for HLA/peptide targets, which can be readily combined with a new generation of anti-CD3e-specific DARPins.
External linksiScience / PubMed:41321628 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.76 - 3.1 Å
Structure data

50336

9fe1

EMDB-50336, PDB-9fe1:
Cryo-EM structure of the ternary DARPin NY_1/HLA-A0201/NY-ESO1 complex.
Method: EM (single particle) / Resolution: 3.1 Å

PDB-9epa:
Crystal structure of DARPin NY_1
Method: X-RAY DIFFRACTION / Resolution: 1.76 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsIMMUNE SYSTEM / DARPin targeting MHC molecules in complex with tumor-associated peptide antigens

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