Fig. 3: Anti-Siglec-15 blocking mAb 5G12 competes for the sialic acid-binding site of Siglec-15. | Nature Communications

Fig. 3: Anti-Siglec-15 blocking mAb 5G12 competes for the sialic acid-binding site of Siglec-15.

From: Structural insights into Siglec-15 reveal glycosylation dependency for its interaction with T cells through integrin CD11b

Fig. 3

a Representative flow cytometry histograms of activated CD8+ and CD4+ human T cells showing the binding of recombinant Siglec-15-Fc in the presence or absence of anti-Siglec-15 5G12 Fab. Here, secondary control means that only an anti-Fc detector antibody, but not recombinant Fc-chimera protein was added to the sample. b Bar graphs show Siglec-15-Fc binding to human T cells in the presence or absence of 5G12 Fab (CD4+: 0.0001, CD8+: 0.0002, n = 4 donors). Errors bars denote SEM. ***p < 0.001 as determined by two-tailed, unpaired Student’s t test. c Competition of 3′SL (left)/6′SL (right) and 5G12 mAb for the same binding site of Siglec-15. Source data are provided as a Source Data file.

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