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

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 system. Increased...

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Auteurs principaux: Mark Austin, Daniel Burschowsky, Denice T.Y. Chan, Lesley Jenkinson, Stuart Haynes, Agata Diamandakis, Chitra Seewooruthun, Alexandra Addyman, Sebastian Fiedler, Stephanie Ryman, Jessica Whitehouse, Louise H. Slater, Andreas V. Hadjinicolaou, Uzi Gileadi, Ellen Gowans, Yoko Shibata, Michelle Barnard, Teresa Kaserer, Pooja Sharma, Nadia M. Luheshi, Robert W. Wilkinson, Tristan J. Vaughan, Sarah V. Holt, Vincenzo Cerundolo, Mark D. Carr, Maria A. T. Groves
Format: Artigo
Langue:Inglês
Publié: Taylor & Francis Group 2020-01-01
Collection:mAbs
Sujets:
ARG2
Arginase 2
antibody co-crystal structure
phage display selections
cancer therapeutics
ARG2 epitope
Accès en ligne:https://www.tandfonline.com/doi/10.1080/19420862.2020.1801230
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