Fig. 2: Non-competitive recognition of CD73 epitopes by mAbs HB0038 and HB0039. | Nature Communications

Fig. 2: Non-competitive recognition of CD73 epitopes by mAbs HB0038 and HB0039.

From: An antibody cocktail targeting two different CD73 epitopes enhances enzyme inhibition and tumor control

Fig. 2

A Hydrogen-deuterium exchange (HDX) identified the epitopes of HB0038 and HB0039 on CD73. These were then mapped onto the CD73 structure (PDB code: 4H1Y) via PyMOL. B–K Time-resolved SPR analysis detailing affinity between HB0038 and CD73 wide type (WT) and its mutants. All CD73 residues identified by HDX analysis potentially involved in HB0038 binding were mutated to Ala individually and were assessed for their contribution to HB0038 binding. The SPR profile of HB0038 against specific CD73 WT and CD73 mutations in the HDX epitope study. L–Q As in (B–K), but between HB0039 and CD73.

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