The N-linked glycosylations of TIGIT Asn 32 and Asn 101 facilitate PVR/TIGIT interaction.

Although the PVR/TIGIT immune checkpoint axis has been suggested as a promising target for cancer immunotherapy and multiple TIGIT-targeting therapies are undergoing clinical trials, the underlying regulatory mechanisms of PVR/TIGIT interaction remain inconclusive. Here we show that TIGIT N-glycosylations are critical for maintaining the interaction between TIGIT and PVR. TIGIT has two N-glycosylation residues, N32 and N101. N-glycosylation on N101 of TIGIT and, to less extent, on N32, play potent roles in PVR binding. Taken together, these findings suggest that the N-glycosylation sites on TIGIT, especially residue N101, may be potential targets for PVR/TIGIT immune checkpoint blockade.
Competing Interests: Declaration of competing interest The authors declare no conflicts of interest regarding this manuscript.
(Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)