ArticleMolecular therapy : the journal of the American Society of Gene Therapy2025
Structure-guided engineering of CD112 receptor variants for optimized immunotherapy.
Article in Molecular therapy : the journal of the American Society of Gene Therapy, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
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Who cites it
1 citing paper in PubMed.
- Negative Immune Checkpoint Inhibitors.Pharmaceutics · 2025Review
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Authors and funding
11 authors.
Funding
Abstract
The immune checkpoint protein, CD112 receptor (CD112R, also known as PVRIG), suppresses T and natural killer (NK) cell activation upon binding to tumor-expressed CD112 (Nectin-2) ligands. Here, we determine the structure of the CD112-CD112R complex and use it to guide the engineering of multiple CD112-targeting immunotherapy candidates. The 2.2 Å-resolution crystal structure reveals an antiparallel, lock-and-key binding mode in which CD112R disrupts CD112 homodimerization. Structural analysis informed directed evolution campaigns focused on remodeling the CD112-CD112R interface, resulting in the isolation of CD112R mutants with greatly increased expression and CD112-binding affinity. The highest-affinity variant, CD112R
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Registered trials
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