Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein
Identifieur interne : 000C74 ( Main/Exploration ); précédent : 000C73; suivant : 000C75Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein
Auteurs : Si Min Zhang [Singapour, 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 [ 1357-2725 ] ; 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
Url:
DOI: 10.1016/j.biocel.2018.05.012
PubMed: 29800727
PubMed Central: 7108413
Affiliations:
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Medicine, Karolinska Institutet</wicri:regionArea><wicri:noRegion>Karolinska Institutet</wicri:noRegion></affiliation></author><author><name sortKey="Liao, Ying" sort="Liao, Ying" uniqKey="Liao Y" first="Ying" last="Liao">Ying Liao</name><affiliation wicri:level="1"><nlm:aff id="aff0015">Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai</wicri:regionArea><wicri:noRegion>Shanghai</wicri:noRegion></affiliation></author><author><name sortKey="Neo, Tuan Ling" sort="Neo, Tuan Ling" uniqKey="Neo T" first="Tuan Ling" last="Neo">Tuan Ling Neo</name><affiliation wicri:level="1"><nlm:aff id="aff0005">School of Biological Sciences, Nanyang Technological University, Singapore</nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Sciences, Nanyang Technological University</wicri:regionArea><wicri:noRegion>Nanyang Technological University</wicri:noRegion></affiliation></author><author><name sortKey="Lu, Yanning" sort="Lu, Yanning" uniqKey="Lu Y" first="Yanning" last="Lu">Yanning Lu</name><affiliation wicri:level="1"><nlm:aff id="aff0005">School of Biological Sciences, Nanyang Technological University, Singapore</nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Sciences, Nanyang Technological University</wicri:regionArea><wicri:noRegion>Nanyang Technological University</wicri:noRegion></affiliation></author><author><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name><affiliation wicri:level="1"><nlm:aff id="aff0005">School of Biological Sciences, Nanyang Technological University, Singapore</nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Sciences, Nanyang Technological University</wicri:regionArea><wicri:noRegion>Nanyang Technological University</wicri:noRegion></affiliation></author><author><name sortKey="Vahlne, Anders" sort="Vahlne, Anders" uniqKey="Vahlne A" first="Anders" last="Vahlne">Anders Vahlne</name><affiliation wicri:level="1"><nlm:aff id="aff0010">Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institutet, Sweden</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea>Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institutet</wicri:regionArea><wicri:noRegion>Karolinska Institutet</wicri:noRegion></affiliation></author><author><name sortKey="Tam, James P" sort="Tam, James P" uniqKey="Tam J" first="James P." last="Tam">James P. Tam</name><affiliation wicri:level="1"><nlm:aff id="aff0005">School of Biological Sciences, Nanyang Technological University, Singapore</nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Sciences, Nanyang Technological University</wicri:regionArea><wicri:noRegion>Nanyang Technological University</wicri:noRegion></affiliation></author></analytic><series><title level="j">The International Journal of Biochemistry & Cell Biology</title><idno type="ISSN">1357-2725</idno><idno type="eISSN">1878-5875</idno><imprint><date when="2018">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Amyloidogenic Proteins (chemistry)</term><term>Amyloidogenic Proteins (genetics)</term><term>Amyloidogenic Proteins (metabolism)</term><term>Animals</term><term>Gene Expression</term><term>HEK293 Cells</term><term>Hemagglutinins (genetics)</term><term>Hemagglutinins (metabolism)</term><term>Humans</term><term>Peptide Library</term><term>Peptides (chemical synthesis)</term><term>Peptides (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (chemistry)</term><term>Sf9 Cells</term><term>Solid-Phase Synthesis Techniques</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (genetics)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Spodoptera</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Banque de peptides</term><term>Cellules HEK293</term><term>Cellules Sf9</term><term>Expression des gènes</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Glycoprotéine de spicule des coronavirus (génétique)</term><term>Glycoprotéine de spicule des coronavirus (métabolisme)</term><term>Humains</term><term>Hémagglutinines (génétique)</term><term>Hémagglutinines (métabolisme)</term><term>Liaison aux protéines</term><term>Peptides (métabolisme)</term><term>Peptides (synthèse chimique)</term><term>Protéines amyloïdogènes ()</term><term>Protéines amyloïdogènes (génétique)</term><term>Protéines amyloïdogènes (métabolisme)</term><term>Protéines de fusion recombinantes ()</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Spodoptera</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Techniques de synthèse en phase solide</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloidogenic Proteins</term><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amyloidogenic Proteins</term><term>Hemagglutinins</term><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloidogenic Proteins</term><term>Hemagglutinins</term><term>Peptides</term><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term><term>Hémagglutinines</term><term>Protéines amyloïdogènes</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term><term>Hémagglutinines</term><term>Peptides</term><term>Protéines amyloïdogènes</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Peptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Gene Expression</term><term>HEK293 Cells</term><term>Humans</term><term>Peptide Library</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Sf9 Cells</term><term>Solid-Phase Synthesis Techniques</term><term>Spodoptera</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Banque de peptides</term><term>Cellules HEK293</term><term>Cellules Sf9</term><term>Expression des gènes</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Protéines amyloïdogènes</term><term>Protéines de fusion recombinantes</term><term>Spodoptera</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Techniques de synthèse en phase solide</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>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 <italic>in vitro</italic> 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.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Azriel, R" uniqKey="Azriel R">R. Azriel</name></author><author><name sortKey="Gazit, E" uniqKey="Gazit E">E. Gazit</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Azzarito, V" uniqKey="Azzarito V">V. Azzarito</name></author><author><name sortKey="Long, K" uniqKey="Long K">K. Long</name></author><author><name sortKey="Murphy, N S" uniqKey="Murphy N">N.S. 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Tam</name></country><country name="Suède"><noRegion><name sortKey="Zhang, Si Min" sort="Zhang, Si Min" uniqKey="Zhang S" first="Si Min" last="Zhang">Si Min Zhang</name></noRegion><name sortKey="Vahlne, Anders" sort="Vahlne, Anders" uniqKey="Vahlne A" first="Anders" last="Vahlne">Anders Vahlne</name></country><country name="République populaire de Chine"><noRegion><name sortKey="Liao, Ying" sort="Liao, Ying" uniqKey="Liao Y" first="Ying" last="Liao">Ying Liao</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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