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|Title:||Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein||Authors:||Zhang, Si Min
Neo, Tuan Ling
Liu, Ding Xiang
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.||URI:||https://hdl.handle.net/10356/142743||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|
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