Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein
文献类型: 外文期刊
第一作者: Zhang, Si Min
作者: Zhang, Si Min;Neo, Tuan Ling;Lu, Yanning;Liu, Ding Xiang;Tam, James P.;Zhang, Si Min;Vahlne, Anders;Liao, Ying
作者机构:
关键词: Steric beta-zipper; SARS-CoV spike protein; Class I viral fusion glycoprotein; self-binding peptides; viral detection
期刊名称:INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY ( 影响因子:5.085; 五年影响因子:4.407 )
ISSN: 1357-2725
年卷期: 2018 年 101 卷
页码:
收录情况: SCI
摘要: Self-binding peptides containing zipper-like sequences, such as the Leu/Ile zipper sequence within the coiled coil regions of proteins and the cross-beta spine stenc zippers within the amyloid-like fibrils, could bind to the protein- of-origin through homophilic sequence-specific zipper motifs. These self-binding sequences represent opportu nities for the development of biochemical tools and/or therapeutics. Here, we report on the identification of a putative self-binding beta-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 stenc beta-zipper formation. Peptide C6 containing the Cluster I consensus sequence was shown to oligomenze 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 beta-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.
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