Specific Unbinding Forces between Mutated Human P-Selectin Glycoprotein Ligand-1 and Viral Protein-1 Measured Using Force Spectroscopy

Chen Chu Wang, Kundan Sivashanmugan, Chung Ku Chen, Jian Ren Hong, Wei I. Sung, Jiunn Der Liao, Yuh Shyong Yang

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)5290-5295
Number of pages6
JournalJournal of Physical Chemistry Letters
Volume8
Issue number21
DOIs
Publication statusPublished - 2017 Nov 2

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Physical and Theoretical Chemistry

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