1 research outputs found
Specific Unbinding Forces Between Mutated Human P‑Selectin Glycoprotein Ligand‑1 and Viral Protein‑1 Measured Using Force Spectroscopy
Protein tyrosine
sulfation (PTS) is a key modulator of extracellular
protein–protein interaction (PPI), which regulates principal
biological processes. For example, the capsid protein VP1 of enterovirus
71 (EV71) specifically interacts with sulfated P-selectin glycoprotein
ligand-1 (PSGL-1) to facilitate virus invasion. Currently available
methods cannot be used to directly observe PTS-induced PPI. In this
study, atomic force microscopy was used to measure the interaction
between sulfated or mutated PSGL-1 and VP1. We found that the binding
strength increased by 6.7-fold following PTS treatment on PSGL-1 with
a specific antisulfotyrosine antibody. Similar results were obtained
when the antisulfotyrosine antibody was replaced with the VP1 protein
of EV71; however, the interaction forces of VP1 were only approximately
one-third of those of the antisulfotyrosine antibody. We also found
that PTS on the tyrosine-51 residue of glutathione S-transferases
fusion-PSGL-1 was mainly responsible for the PTS-induced PPI. Our
results contribute to the fundamental understanding of PPI regulated
through PTS