Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein.
Identifieur interne : 000999 ( PubMed/Checkpoint ); précédent : 000998; suivant : 000A00Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein.
Auteurs : Si Min Zhang [Suède] ; Ying Liao [République populaire de Chine] ; Tuan Ling Neo [Singapour] ; Yanning Lu [Singapour] ; Ding Xiang Liu [Singapour] ; Anders Vahlne [Suède] ; James P. Tam [Singapour]Source :
- The international journal of biochemistry & cell biology [ 1878-5875 ] ; 2018.
Descripteurs français
- KwdFr :
- Animaux, Banque de peptides, Cellules HEK293, Cellules Sf9, Expression des gènes, Glycoprotéine de spicule des coronavirus (), Glycoprotéine de spicule des coronavirus (génétique), Glycoprotéine de spicule des coronavirus (métabolisme), Humains, Hémagglutinines (génétique), Hémagglutinines (métabolisme), Liaison aux protéines, Peptides (métabolisme), Peptides (synthèse chimique), Protéines amyloïdogènes (), Protéines amyloïdogènes (génétique), Protéines amyloïdogènes (métabolisme), Protéines de fusion recombinantes (), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Spodoptera, Structure secondaire des protéines, Séquence d'acides aminés, Techniques de synthèse en phase solide, Virus du SRAS ().
- MESH :
- génétique : Glycoprotéine de spicule des coronavirus, Hémagglutinines, Protéines amyloïdogènes, Protéines de fusion recombinantes.
- métabolisme : Glycoprotéine de spicule des coronavirus, Hémagglutinines, Peptides, Protéines amyloïdogènes, Protéines de fusion recombinantes.
- synthèse chimique : Peptides.
- Animaux, Banque de peptides, Cellules HEK293, Cellules Sf9, Expression des gènes, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Protéines amyloïdogènes, Protéines de fusion recombinantes, Spodoptera, Structure secondaire des protéines, Séquence d'acides aminés, Techniques de synthèse en phase solide, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amyloidogenic Proteins (chemistry), Amyloidogenic Proteins (genetics), Amyloidogenic Proteins (metabolism), Animals, Gene Expression, HEK293 Cells, Hemagglutinins (genetics), Hemagglutinins (metabolism), Humans, Peptide Library, Peptides (chemical synthesis), Peptides (metabolism), Protein Binding, Protein Structure, Secondary, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (chemistry), Sf9 Cells, Solid-Phase Synthesis Techniques, Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Spodoptera.
- MESH :
- chemical , chemical synthesis : Peptides.
- chemical , chemistry : Amyloidogenic Proteins, Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- chemical , genetics : Amyloidogenic Proteins, Hemagglutinins, Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Amyloidogenic Proteins, Hemagglutinins, Peptides, Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- Amino Acid Sequence, Animals, Gene Expression, HEK293 Cells, Humans, Peptide Library, Protein Binding, Protein Structure, Secondary, Sf9 Cells, Solid-Phase Synthesis Techniques, Spodoptera.
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.
DOI: 10.1016/j.biocel.2018.05.012
PubMed: 29800727
Affiliations:
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pubmed:29800727Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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<DateCompleted><Year>2019</Year>
<Month>03</Month>
<Day>28</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>15</Day>
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<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-5875</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>101</Volume>
<PubDate><Year>2018</Year>
<Month>08</Month>
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<Title>The international journal of biochemistry & cell biology</Title>
<ISOAbbreviation>Int. J. Biochem. Cell Biol.</ISOAbbreviation>
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<ArticleTitle>Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein.</ArticleTitle>
<Pagination><MedlinePgn>103-112</MedlinePgn>
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<Abstract><AbstractText>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.</AbstractText>
<CopyrightInformation>Copyright © 2018 Elsevier Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Si Min</ForeName>
<Initials>SM</Initials>
<AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore; Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institutet, Sweden.</Affiliation>
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<ForeName>Ying</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Neo</LastName>
<ForeName>Tuan Ling</ForeName>
<Initials>TL</Initials>
<AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Lu</LastName>
<ForeName>Yanning</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Ding Xiang</ForeName>
<Initials>DX</Initials>
<AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Vahlne</LastName>
<ForeName>Anders</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institutet, Sweden.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tam</LastName>
<ForeName>James P</ForeName>
<Initials>JP</Initials>
<AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore. Electronic address: jptam@ntu.edu.sg.</Affiliation>
</AffiliationInfo>
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<Month>05</Month>
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