Fig. 6: Antibody-CS complexing depends on oligomerization on a long CS chain. | Nature Communications

Fig. 6: Antibody-CS complexing depends on oligomerization on a long CS chain.

From: Tumor-agnostic cancer therapy using antibodies targeting oncofetal chondroitin sulfate

Fig. 6

a Mass photometry contrasts of dimerized antibody fragments (B1, C9, and F8) analyzed alone (red) or in combination with soluble CSA or CSC (green). Soluble uncomplexed CS (yellow) was analyzed as a control. b 2D classification of B1 Fab:CSA complex from cryo-EM. c Cryo-EM density map depicting CS glycan chains (red) traversing across B1 Fabs in a tetramer complex. d Heavy chain:heavy chain homotypic interactions of B1 Fab. e Structure of B1 Fab interaction with CSA showing electrostatic surface potential of the complex. Above, a zoom-in of the dashed box is shown. f Single-cell RNAseq analysis of CS-related genes in a non-small lung carcinoma (NSCLC) transcriptome atlas (left and right) and a schematic overview of studied CS synthesis pathways (middle).

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