TY - JOUR
T1 - 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
AU - Sivashanmugan, Kundan
AU - Lee, Han
AU - Liao, Jiunn Der
AU - Wang, Chen Chu
AU - Lin, Chen Hsueh
AU - Yang, Yuh Shyong
AU - Sitjar, Jaya
N1 - Funding Information:
This research received grant from the Headquarter of University Advancement at National Cheng Kung University (NCKU), sponsored by the Taiwan Ministry of Science and Technology under Grant Nos. 108-2218-E-006-054-MY3, 106-2811-E-066-061 and 108-2811-E-006-535. The funder had no role in study design, data collection, and analysis, decision to publish, or preparation of the manuscript.
Publisher Copyright:
© 2020 by the authors.
PY - 2020/4/1
Y1 - 2020/4/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85083839013&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85083839013&partnerID=8YFLogxK
U2 - 10.3390/coatings10040403
DO - 10.3390/coatings10040403
M3 - Article
AN - SCOPUS:85083839013
SN - 2079-6412
VL - 10
JO - Coatings
JF - Coatings
IS - 4
M1 - 403
ER -