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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
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