The N-linked glycosylations of TIGIT Asn32 and Asn101 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.
['Lin|Yu-Xi|YX|', 'Hung|Mien-Chie|MC|', 'Hsu|Jye-Lin|JL|', 'Hsu|Jung-Mao|JM|']
D000595:Amino Acid Sequence D001216:Asparagine D006031:Glycosylation D057809:HEK293 Cells D006801:Humans D011485:Protein Binding D011971:Receptors, Immunologic D011991:Receptors, Virus
N-linked glycosylation TIGIT PVR CD155 VSTM3