Please use this identifier to cite or link to this item:
Title: Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein
Authors: Zhang, Si Min
Liao, Ying
Neo, Tuan Ling
Lu, Yanning
Liu, Ding Xiang
Vahlne, Anders
Tam, James Pingkwan
Keywords: Science::Biological sciences
Issue Date: 2018
Source: Zhang, S. M., Liao, Y., Neo, T. L., Lu, Y., Liu, D. X., Vahlne, A., & Tam, J. P. (2018). Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein. International Journal of Biochemistry and Cell Biology, 101, 103-112. doi:10.1016/j.biocel.2018.05.012
Journal: International Journal of Biochemistry and Cell Biology
Abstract: Self-binding peptides containing zipper-like sequences, such as the Leu/Ile zipper sequence within the coiled coil regions of proteins and the cross-β spine steric zippers within the amyloid-like fibrils, could bind to the protein-of-origin through homophilic sequence-specific zipper motifs. These self-binding sequences represent opportunities for the development of biochemical tools and/or therapeutics. Here, we report on the identification of a putative self-binding β-zipper-forming peptide within the severe acute respiratory syndrome-associated coronavirus spike (S) protein and its application in viral detection. Peptide array scanning of overlapping peptides covering the entire length of S protein identified 34 putative self-binding peptides of six clusters, five of which contained octapeptide core consensus sequences. The Cluster I consensus octapeptide sequence GINITNFR was predicted by the Eisenberg's 3D profile method to have high amyloid-like fibrillation potential through steric β-zipper formation. Peptide C6 containing the Cluster I consensus sequence was shown to oligomerize and form amyloid-like fibrils. Taking advantage of this, C6 was further applied to detect the S protein expression in vitro by fluorescence staining. Meanwhile, the coiled-coil-forming Leu/Ile heptad repeat sequences within the S protein were under-represented during peptide array scanning, in agreement with that long peptide lengths were required to attain high helix-mediated interaction avidity. The data suggest that short β-zipper-like self-binding peptides within the S protein could be identified through combining the peptide scanning and predictive methods, and could be exploited as biochemical detection reagents for viral infection.
ISSN: 1357-2725
DOI: 10.1016/j.biocel.2018.05.012
Rights: © 2018 Elsevier Ltd. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

Citations 50

Updated on Jan 31, 2023

Web of ScienceTM
Citations 50

Updated on Jan 31, 2023

Page view(s)

Updated on Feb 3, 2023

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.