Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein
Identifieur interne : 000673 ( PascalFrancis/Corpus ); précédent : 000672; suivant : 000674Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein
Auteurs : Bruno Jr Sainz ; Joshua M. Rausch ; William R. Gallaher ; Robert F. Garry ; William C. WimleySource :
- Journal of virology [ 0022-538X ] ; 2005.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
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 (SAItSWW-I and SARSWW-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 SARSWW-I peptide strongly partitioned into the membranes of large unilamellar vesicles (LUV), adopting a β-sheet structure. Likewise, only SA========Rgr;SWW-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 SA========Rgr;SWW-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.
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NO : | PASCAL 05-0250065 INIST |
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ET : | Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein |
AU : | SAINZ (Bruno JR); RAUSCH (Joshua M.); GALLAHER (William R.); GARRY (Robert F.); WIMLEY (William C.) |
AF : | Department of Microbiology and Immunology, Program in Molecular Pathogenesis and Immunity, Tulane University Health Sciences Center/New Orleans, Louisiana 70112/Etats-Unis (1 aut., 4 aut.); Department of Biochemistry, Tulane University Health Sciences Center/New Orleans, Louisiana 70112/Etats-Unis (2 aut., 5 aut.); Department of Microbiology, Immunology and Parasitology, Louisiana State University Health Sciences Center/New Orleans, Louisiana 70112/Etats-Unis (3 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2005; Vol. 79; No. 11; Pp. 7195-7206; Bibl. 99 ref. |
LA : | Anglais |
EA : | 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 (SAItSWW-I and SARSWW-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 SARSWW-I peptide strongly partitioned into the membranes of large unilamellar vesicles (LUV), adopting a β-sheet structure. Likewise, only SA========Rgr;SWW-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 SA========Rgr;SWW-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. |
CC : | 002A05C10 |
FD : | Coronavirus; Identification; Peptide; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère |
FG : | Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie |
ED : | Coronavirus; Identification; Peptides; Protein; Microbiology; Virology; Severe acute respiratory syndrome |
EG : | Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease |
SD : | Coronavirus; Identificación; Péptido; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo |
LO : | INIST-13592.354000125436420630 |
ID : | 05-0250065 |
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Pascal:05-0250065Le 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 (SAItS<sub>WW-I</sub>
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<server><NO>PASCAL 05-0250065 INIST</NO>
<ET>Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein</ET>
<AU>SAINZ (Bruno JR); RAUSCH (Joshua M.); GALLAHER (William R.); GARRY (Robert F.); WIMLEY (William C.)</AU>
<AF>Department of Microbiology and Immunology, Program in Molecular Pathogenesis and Immunity, Tulane University Health Sciences Center/New Orleans, Louisiana 70112/Etats-Unis (1 aut., 4 aut.); Department of Biochemistry, Tulane University Health Sciences Center/New Orleans, Louisiana 70112/Etats-Unis (2 aut., 5 aut.); Department of Microbiology, Immunology and Parasitology, Louisiana State University Health Sciences Center/New Orleans, Louisiana 70112/Etats-Unis (3 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2005; Vol. 79; No. 11; Pp. 7195-7206; Bibl. 99 ref.</SO>
<LA>Anglais</LA>
<EA>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 (SAItS<sub>WW-I</sub>
and SARS<sub>WW-II</sub>
) 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<sub>WW-I</sub>
peptide strongly partitioned into the membranes of large unilamellar vesicles (LUV), adopting a β-sheet structure. Likewise, only SA========Rgr;S<sub>WW-I</sub>
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 SA========Rgr;S<sub>WW-I</sub>
, 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.</EA>
<CC>002A05C10</CC>
<FD>Coronavirus; Identification; Peptide; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère</FD>
<FG>Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie</FG>
<ED>Coronavirus; Identification; Peptides; Protein; Microbiology; Virology; Severe acute respiratory syndrome</ED>
<EG>Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease</EG>
<SD>Coronavirus; Identificación; Péptido; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo</SD>
<LO>INIST-13592.354000125436420630</LO>
<ID>05-0250065</ID>
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