Mutated human p-selectin glycoprotein ligand-1 and viral protein-1 of enterovirus 71 interactions on Au nanoplasmonic substrate for specific recognition by surface-enhanced raman spectroscopy

Kundan Sivashanmugan, Han Lee, Jiunn Der Liao, Chen Chu Wang, Chen Hsueh Lin, Yuh Shyong Yang, Jaya Sitjar

Research output: Contribution to journalArticle

Abstract

Protein tyrosine sulfation is a common post-translational modification that stimulates intercellular or extracellular protein-protein interactions and is responsible for various important biological processes, including coagulation, inflammation, and virus infections. Recently, human P-selectin glycoprotein ligand-1 (PSGL-1) has been shown to serve as a functional receptor for enterovirus 71 (EV71). It has been proposed that the capsid viral protein VP1 of EV71 is directly involved in this specific interaction with sulfated or mutated PSGL-1. Surface-enhanced Raman spectroscopy (SERS) is used to distinguish PSGL-1 and VP1 interactions on an Au nanoporous substrate and identify specific VP1 interaction positions of tyrosine residue sites (46, 48, and 51). The three tyrosine sites in PSGL-1 were replaced by phenylalanine (F), as determined using SERS. A strong phenylalanine SERS signal was obtained in three regions of the mutated protein on the nanoporous substrate. The mutated protein positions at (51F) and (48F, 51F) produced a strong SERS peak at 1599-1666 cm-1, which could be related to a binding with the mutated protein and anti-sulfotyrosine interactions on the nanoporous substrate. A strong SERS effect of the mutated protein and VP1 interactions appeared at (48F), (51F), and (46F, 48F). In these positions, there was less interaction with VP1, as indicated by a strong phenylalanine signal from the mutated protein.

Original languageEnglish
Article number403
JournalCoatings
Volume10
Issue number4
DOIs
Publication statusPublished - 2020 Apr 1

All Science Journal Classification (ASJC) codes

  • Surfaces and Interfaces
  • Surfaces, Coatings and Films
  • Materials Chemistry

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