Structural and functional characterization of C0021158, a high-affinity monoclonal antibody that inhibits Arginase 2 function via a novel non-competitive mechanism of action

• Main Authors: Mark Austin (Author), Daniel Burschowsky (Author), Denice T.Y. Chan (Author), Lesley Jenkinson (Author), Stuart Haynes (Author), Agata Diamandakis (Author), Chitra Seewooruthun (Author), Alexandra Addyman (Author), Sebastian Fiedler (Author), Stephanie Ryman (Author), Jessica Whitehouse (Author), Louise H. Slater (Author), Andreas V. Hadjinicolaou (Author), Uzi Gileadi (Author), Ellen Gowans (Author), Yoko Shibata (Author), Michelle Barnard (Author), Teresa Kaserer (Author), Pooja Sharma (Author), Nadia M. Luheshi (Author), Robert W. Wilkinson (Author), Tristan J. Vaughan (Author), Sarah V. Holt (Author), Vincenzo Cerundolo (Author), Mark D. Carr (Author), Maria A. T. Groves (Author)
• Format: Book
• Published: Taylor & Francis Group, 2020-01-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

Arginase 2 (ARG2) is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of L-arginine. The dysregulated expression of ARG2 within specific tumor microenvironments generates an immunosuppressive niche that effectively renders the tumor 'invisible' to the host's immune sy...