Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction.
Identifieur interne : 001297 ( Ncbi/Merge ); précédent : 001296; suivant : 001298Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction.
Auteurs : Tin-Yun Ho [Taïwan] ; Shih-Lu Wu ; Jaw-Chyun Chen ; Yen-Chiao Wei ; Shin-Ei Cheng ; Yung-Hsien Chang ; Hsu-Jan Liu ; Chien-Yun HsiangSource :
- Antiviral research [ 0166-3542 ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Biotinylation, Cellules Vero, Données de séquences moléculaires, Facteurs de transcription (antagonistes et inhibiteurs), Facteurs de transcription (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (antagonistes et inhibiteurs), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Peptides (), Peptides (métabolisme), Peptides (synthèse chimique), Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (antagonistes et inhibiteurs), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines de liaison à l'ADN (antagonistes et inhibiteurs), Protéines de liaison à l'ADN (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Test ELISA, Virus du SRAS (métabolisme), Virus du SRAS (pathogénicité).
- MESH :
- antagonistes et inhibiteurs : Facteurs de transcription, Glycoprotéines membranaires, Protéines de Saccharomyces cerevisiae, Protéines de l'enveloppe virale, Protéines de liaison à l'ADN.
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes.
- métabolisme : Facteurs de transcription, Glycoprotéines membranaires, Peptides, Protéines de Saccharomyces cerevisiae, Protéines de l'enveloppe virale, Protéines de liaison à l'ADN, Protéines recombinantes, Virus du SRAS.
- pathogénicité : Virus du SRAS.
- synthèse chimique : Peptides.
- virologie : Syndrome respiratoire aigu sévère.
- Animaux, Biotinylation, Cellules Vero, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Peptides, Protéines de l'enveloppe virale, Séquence d'acides aminés, Test ELISA.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Biotinylation, Chlorocebus aethiops, DNA-Binding Proteins (antagonists & inhibitors), DNA-Binding Proteins (metabolism), Enzyme-Linked Immunosorbent Assay, Humans, Membrane Glycoproteins (antagonists & inhibitors), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Peptides (chemical synthesis), Peptides (chemistry), Peptides (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (metabolism), SARS Virus (pathogenicity), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (metabolism), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Transcription Factors (antagonists & inhibitors), Transcription Factors (metabolism), Vero Cells, Viral Envelope Proteins (antagonists & inhibitors), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : DNA-Binding Proteins, Membrane Glycoproteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Viral Envelope Proteins.
- chemical , chemical synthesis : Peptides.
- chemical , chemistry : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : DNA-Binding Proteins, Membrane Glycoproteins, Peptides, Recombinant Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Viral Envelope Proteins.
- metabolism : SARS Virus.
- pathogenicity : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Animals, Biotinylation, Chlorocebus aethiops, Enzyme-Linked Immunosorbent Assay, Humans, Molecular Sequence Data, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel coronavirus (SARS-CoV). The binding of SARS-CoV spike (S) protein to cellular angiotensin-converting enzyme 2 (ACE2) is the first step in SARS-CoV infection. Therefore, we assayed the inhibitory effects of small peptides derived from S protein on the binding of S protein to ACE2 and on the S-protein-pseudotyped retrovirus infectivity. SP-4 (residues 192-203), SP-8 (residues 483-494), and SP-10 (residues 668-679) significantly blocked the interaction between S protein and ACE2 by biotinylated enzyme-linked immunosorbent assay, with IC(50) values of 4.30 +/- 2.18, 6.99 +/- 0.71, and 1.88 +/- 0.52 nmol, respectively. Peptide scanning suggested the region spanning residues 660-683 might act as a receptor-binding domain. SP-10 blocked both binding of the S protein and infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. In conclusion, this is the first report of small peptides designed to disrupt the binding of SARS-CoV S protein to ACE2. Our findings suggest that SP-10 may be developed as an anti-SARS-CoV agent for the treatment of SARS-CoV infection.
DOI: 10.1016/j.antiviral.2005.10.005
PubMed: 16337697
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002416
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pubmed:16337697Le document en format XML
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<term>DNA-Binding Proteins (antagonists & inhibitors)</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Humans</term>
<term>Membrane Glycoproteins (antagonists & inhibitors)</term>
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<term>Animals</term>
<term>Biotinylation</term>
<term>Chlorocebus aethiops</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel coronavirus (SARS-CoV). The binding of SARS-CoV spike (S) protein to cellular angiotensin-converting enzyme 2 (ACE2) is the first step in SARS-CoV infection. Therefore, we assayed the inhibitory effects of small peptides derived from S protein on the binding of S protein to ACE2 and on the S-protein-pseudotyped retrovirus infectivity. SP-4 (residues 192-203), SP-8 (residues 483-494), and SP-10 (residues 668-679) significantly blocked the interaction between S protein and ACE2 by biotinylated enzyme-linked immunosorbent assay, with IC(50) values of 4.30 +/- 2.18, 6.99 +/- 0.71, and 1.88 +/- 0.52 nmol, respectively. Peptide scanning suggested the region spanning residues 660-683 might act as a receptor-binding domain. SP-10 blocked both binding of the S protein and infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. In conclusion, this is the first report of small peptides designed to disrupt the binding of SARS-CoV S protein to ACE2. Our findings suggest that SP-10 may be developed as an anti-SARS-CoV agent for the treatment of SARS-CoV infection.</div>
</front>
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<DateCompleted><Year>2006</Year>
<Month>06</Month>
<Day>06</Day>
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<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>15</Day>
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<Title>Antiviral research</Title>
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<ArticleTitle>Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction.</ArticleTitle>
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<Abstract><AbstractText>Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel coronavirus (SARS-CoV). The binding of SARS-CoV spike (S) protein to cellular angiotensin-converting enzyme 2 (ACE2) is the first step in SARS-CoV infection. Therefore, we assayed the inhibitory effects of small peptides derived from S protein on the binding of S protein to ACE2 and on the S-protein-pseudotyped retrovirus infectivity. SP-4 (residues 192-203), SP-8 (residues 483-494), and SP-10 (residues 668-679) significantly blocked the interaction between S protein and ACE2 by biotinylated enzyme-linked immunosorbent assay, with IC(50) values of 4.30 +/- 2.18, 6.99 +/- 0.71, and 1.88 +/- 0.52 nmol, respectively. Peptide scanning suggested the region spanning residues 660-683 might act as a receptor-binding domain. SP-10 blocked both binding of the S protein and infectivity of S protein-pseudotyped retrovirus to Vero E6 cells. In conclusion, this is the first report of small peptides designed to disrupt the binding of SARS-CoV S protein to ACE2. Our findings suggest that SP-10 may be developed as an anti-SARS-CoV agent for the treatment of SARS-CoV infection.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ho</LastName>
<ForeName>Tin-Yun</ForeName>
<Initials>TY</Initials>
<AffiliationInfo><Affiliation>Molecular Biology Laboratory, Graduate Institute of Chinese Medical Science, China Medical University, Taichung, Taiwan.</Affiliation>
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<ForeName>Shih-Lu</ForeName>
<Initials>SL</Initials>
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<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Jaw-Chyun</ForeName>
<Initials>JC</Initials>
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<Author ValidYN="Y"><LastName>Wei</LastName>
<ForeName>Yen-Chiao</ForeName>
<Initials>YC</Initials>
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<Author ValidYN="Y"><LastName>Cheng</LastName>
<ForeName>Shin-Ei</ForeName>
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<Author ValidYN="Y"><LastName>Chang</LastName>
<ForeName>Yung-Hsien</ForeName>
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<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Hsu-Jan</ForeName>
<Initials>HJ</Initials>
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<Author ValidYN="Y"><LastName>Hsiang</LastName>
<ForeName>Chien-Yun</ForeName>
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