SrasV1, Ncbi, Merge, bibRecord, 000F45

Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein.

Identifieur interne : 000F45 ( Ncbi/Merge ); précédent : 000F44; suivant : 000F46

Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein.

Auteurs : Bruno Sainz [États-Unis] ; Joshua M. Rausch ; William R. Gallaher ; Robert F. Garry ; William C. Wimley

Source :

Journal of virology [ 0022-538X ] ; 2005.

RBID : pubmed:15890958

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Circular Dichroism, In Vitro Techniques, Liposomes, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Membrane Lipids (chemistry), Models, Molecular, Molecular Sequence Data, Peptide Fragments (chemistry), Peptide Fragments (genetics), Peptide Fragments (physiology), Protein Structure, Secondary, Protein Subunits, SARS Virus (genetics), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology), Viral Fusion Proteins (chemistry), Viral Fusion Proteins (genetics), Viral Fusion Proteins (physiology).
MESH :
- chemical , chemistry : Membrane Glycoproteins, Membrane Lipids, Peptide Fragments, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , genetics : Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , physiology : Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical : Liposomes, Protein Subunits, Spike Glycoprotein, Coronavirus.
- genetics : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Circular Dichroism, In Vitro Techniques, Membrane Fusion, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary.

Abstract

Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is a newly identified member of the family Coronaviridae and poses a serious public health threat. Recent studies indicated that the SARS-CoV viral spike glycoprotein is a class I viral fusion protein. A fusion peptide present at the N-terminal region of class I viral fusion proteins is believed to initiate viral and cell membrane interactions and subsequent fusion. Although the SARS-CoV fusion protein heptad repeats have been well characterized, the fusion peptide has yet to be identified. Based on the conserved features of known viral fusion peptides and using Wimley and White interfacial hydrophobicity plots, we have identified two putative fusion peptides (SARS(WW-I) and SARS(WW-II)) at the N terminus of the SARS-CoV S2 subunit. Both peptides are hydrophobic and rich in alanine, glycine, and/or phenylalanine residues and contain a canonical fusion tripeptide along with a central proline residue. Only the SARS(WW-I) peptide strongly partitioned into the membranes of large unilamellar vesicles (LUV), adopting a beta-sheet structure. Likewise, only SARS(WW-I) induced the fusion of LUV and caused membrane leakage of vesicle contents at peptide/lipid ratios of 1:50 and 1:100, respectively. The activity of this synthetic peptide appeared to be dependent on its amino acid (aa) sequence, as scrambling the peptide rendered it unable to partition into LUV, assume a defined secondary structure, or induce both fusion and leakage of LUV. Based on the activity of SARS(WW-I), we propose that the hydrophobic stretch of 19 aa corresponding to residues 770 to 788 is a fusion peptide of the SARS-CoV S2 subunit.

DOI: 10.1128/JVI.79.11.7195-7206.2005
PubMed: 15890958

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002743
to stream PubMed, to step Curation: 002743
to stream PubMed, to step Checkpoint: 002681

Links to Exploration step

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is a newly identified member of the family Coronaviridae and poses a serious public health threat. Recent studies indicated that the SARS-CoV viral spike glycoprotein is a class I viral fusion protein. A fusion peptide present at the N-terminal region of class I viral fusion proteins is believed to initiate viral and cell membrane interactions and subsequent fusion. Although the SARS-CoV fusion protein heptad repeats have been well characterized, the fusion peptide has yet to be identified. Based on the conserved features of known viral fusion peptides and using Wimley and White interfacial hydrophobicity plots, we have identified two putative fusion peptides (SARS(WW-I) and SARS(WW-II)) at the N terminus of the SARS-CoV S2 subunit. Both peptides are hydrophobic and rich in alanine, glycine, and/or phenylalanine residues and contain a canonical fusion tripeptide along with a central proline residue. Only the SARS(WW-I) peptide strongly partitioned into the membranes of large unilamellar vesicles (LUV), adopting a beta-sheet structure. Likewise, only SARS(WW-I) induced the fusion of LUV and caused membrane leakage of vesicle contents at peptide/lipid ratios of 1:50 and 1:100, respectively. The activity of this synthetic peptide appeared to be dependent on its amino acid (aa) sequence, as scrambling the peptide rendered it unable to partition into LUV, assume a defined secondary structure, or induce both fusion and leakage of LUV. Based on the activity of SARS(WW-I), we propose that the hydrophobic stretch of 19 aa corresponding to residues 770 to 788 is a fusion peptide of the SARS-CoV S2 subunit.</div>
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<Abstract><AbstractText>Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is a newly identified member of the family Coronaviridae and poses a serious public health threat. Recent studies indicated that the SARS-CoV viral spike glycoprotein is a class I viral fusion protein. A fusion peptide present at the N-terminal region of class I viral fusion proteins is believed to initiate viral and cell membrane interactions and subsequent fusion. Although the SARS-CoV fusion protein heptad repeats have been well characterized, the fusion peptide has yet to be identified. Based on the conserved features of known viral fusion peptides and using Wimley and White interfacial hydrophobicity plots, we have identified two putative fusion peptides (SARS(WW-I) and SARS(WW-II)) at the N terminus of the SARS-CoV S2 subunit. Both peptides are hydrophobic and rich in alanine, glycine, and/or phenylalanine residues and contain a canonical fusion tripeptide along with a central proline residue. Only the SARS(WW-I) peptide strongly partitioned into the membranes of large unilamellar vesicles (LUV), adopting a beta-sheet structure. Likewise, only SARS(WW-I) induced the fusion of LUV and caused membrane leakage of vesicle contents at peptide/lipid ratios of 1:50 and 1:100, respectively. The activity of this synthetic peptide appeared to be dependent on its amino acid (aa) sequence, as scrambling the peptide rendered it unable to partition into LUV, assume a defined secondary structure, or induce both fusion and leakage of LUV. Based on the activity of SARS(WW-I), we propose that the hydrophobic stretch of 19 aa corresponding to residues 770 to 788 is a fusion peptide of the SARS-CoV S2 subunit.</AbstractText>
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Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein.

Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein.

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