SrasV1, PascalFrancis, Corpus, bibRecord, 000672

Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus

Identifieur interne : 000672 ( PascalFrancis/Corpus ); précédent : 000671; suivant : 000673

Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus

Auteurs : Bo-Jian Zheng ; YI GUAN ; Ming-Liang He ; HONGZHE SUN ; LANYING DU ; YING ZHENG ; Kin-Ling Wong ; HONGLIN CHEN ; YING CHEN ; LINYU LU ; Julian A. Tanner ; Rory M. Watt ; Neri Niccolai ; Andrea Bernini ; Ottavia Spiga ; Patrick C. Y. Woo ; Hsiang-Fu Kung ; Kwok-Yung Yuen ; Jian-Dong Huang

Source :

Antiviral therapy : (London) [ 1359-6535 ] ; 2005.

RBID : Pascal:05-0250654

Descripteurs français

Pascal (Inist)
- Peptide, Protéine, Virus syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Peptides, Protein, Severe acute respiratory syndrome virus.

Abstract

A novel severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) has been identified as the aetiological agent of SARS. We previously isolated and characterized SARS-CoV and SARS-CoV-like viruses from human and animals, respectively, suggesting that SARS could be transmitted from wild/farmed animals to humans. Comparison of the viral genomes indicated that sequence variation between animal and human isolates existed mainly in the spike (S) gene. We hypothesized that these variations may underlie a change of binding specificity of the S protein to the host cells, permitting viral transmission from animals to humans. Here we report that four 20-mer synthetic peptides (S protein fragments), designed to span these sequence variation hotspots, exhibited significant antiviral activities in a cell line. SARS-CoV infectivity was reduced over 10000-fold through pre-incubation with two of these peptides, while it was completely inhibited in the presence of three peptides. Molecular modelling of the SARS-CoV peplomer suggests that three of these antiviral peptides map to the interfaces between the three monomers of the trimeric peplomer rather than the heptad repeat region from which short peptides are known to inhibit viral entry. Our results revealed novel regions in the spike protein that can be targeted to inhibit viral infection. The peptides identified in this study could be further developed into antiviral drugs.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 1359-6535`
A03		`1`		`@0 Antivir. ther. : (Lond.)`
A05				`@2 10`
A06				`@2 3`
A08	`01`	`1`	`ENG`	`@1 Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus`
A11	`01`	`1`		`@1 ZHENG (Bo-Jian)`
A11	`02`	`1`		`@1 YI GUAN`
A11	`03`	`1`		`@1 HE (Ming-Liang)`
A11	`04`	`1`		`@1 HONGZHE SUN`
A11	`05`	`1`		`@1 LANYING DU`
A11	`06`	`1`		`@1 YING ZHENG`
A11	`07`	`1`		`@1 WONG (Kin-Ling)`
A11	`08`	`1`		`@1 HONGLIN CHEN`
A11	`09`	`1`		`@1 YING CHEN`
A11	`10`	`1`		`@1 LINYU LU`
A11	`11`	`1`		`@1 TANNER (Julian A)`
A11	`12`	`1`		`@1 WATT (Rory M.)`
A11	`13`	`1`		`@1 NICCOLAI (Neri)`
A11	`14`	`1`		`@1 BERNINI (Andrea)`
A11	`15`	`1`		`@1 SPIGA (Ottavia)`
A11	`16`	`1`		`@1 WOO (Patrick C. Y.)`
A11	`17`	`1`		`@1 KUNG (Hsiang-Fu)`
A11	`18`	`1`		`@1 YUEN (Kwok-Yung)`
A11	`19`	`1`		`@1 HUANG (Jian-Dong)`
A14	`01`			`@1 Department of Microbiology, University of Hong Kong @2 Pokfulam @3 HKG @Z 1 aut. @Z 2 aut. @Z 5 aut. @Z 6 aut. @Z 7 aut. @Z 8 aut. @Z 9 aut. @Z 16 aut. @Z 18 aut.`
A14	`02`			`@1 Institute of Molecular Biology, University of Hong Kong @2 Pokfulam @3 HKG @Z 3 aut. @Z 17 aut.`
A14	`03`			`@1 Centre for Emerging Infectious Diseases, Faculty of Medicine, Chinese University of Hong Kong @3 HKG @Z 3 aut. @Z 17 aut.`
A14	`04`			`@1 Department of Chemistry and Open Laboratory of Chemical Biology, University of Hong Kong @2 Pokfulam @3 HKG @Z 4 aut. @Z 12 aut.`
A14	`05`			`@1 Department of Biochemistry, University of Hong Kong @2 Pokfulam @3 HKG @Z 10 aut. @Z 11 aut. @Z 12 aut. @Z 19 aut.`
A14	`06`			`@1 Biomolecular Structure Research Centre, University of Siena @2 Siena @3 ITA @Z 13 aut. @Z 14 aut. @Z 15 aut.`
A20				`@1 393-403`
A21				`@1 2005`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 27047 @5 354000125439640030`
A44				`@0 0000 @1 © 2005 INIST-CNRS. All rights reserved.`
A45				`@0 39 ref.`
A47	`01`	`1`		`@0 05-0250654`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Antiviral therapy : (London)`
A66	`01`			`@0 GBR`
C01	`01`		`ENG`	@0 A novel severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) has been identified as the aetiological agent of SARS. We previously isolated and characterized SARS-CoV and SARS-CoV-like viruses from human and animals, respectively, suggesting that SARS could be transmitted from wild/farmed animals to humans. Comparison of the viral genomes indicated that sequence variation between animal and human isolates existed mainly in the spike (S) gene. We hypothesized that these variations may underlie a change of binding specificity of the S protein to the host cells, permitting viral transmission from animals to humans. Here we report that four 20-mer synthetic peptides (S protein fragments), designed to span these sequence variation hotspots, exhibited significant antiviral activities in a cell line. SARS-CoV infectivity was reduced over 10000-fold through pre-incubation with two of these peptides, while it was completely inhibited in the presence of three peptides. Molecular modelling of the SARS-CoV peplomer suggests that three of these antiviral peptides map to the interfaces between the three monomers of the trimeric peplomer rather than the heptad repeat region from which short peptides are known to inhibit viral entry. Our results revealed novel regions in the spike protein that can be targeted to inhibit viral infection. The peptides identified in this study could be further developed into antiviral drugs.
C02	`01`	`X`		`@0 002B02S05`
C03	`01`	`X`	`FRE`	`@0 Peptide @5 01`
C03	`01`	`X`	`ENG`	`@0 Peptides @5 01`
C03	`01`	`X`	`SPA`	`@0 Péptido @5 01`
C03	`02`	`X`	`FRE`	`@0 Protéine @5 02`
C03	`02`	`X`	`ENG`	`@0 Protein @5 02`
C03	`02`	`X`	`SPA`	`@0 Proteína @5 02`
C03	`03`	`X`	`FRE`	`@0 Virus syndrome respiratoire aigu sévère @2 NW @5 03`
C03	`03`	`X`	`ENG`	`@0 Severe acute respiratory syndrome virus @2 NW @5 03`
C03	`03`	`X`	`SPA`	`@0 Severe acute respiratory syndrome virus @2 NW @5 03`
C07	`01`	`X`	`FRE`	`@0 Coronavirus @2 NW`
C07	`01`	`X`	`ENG`	`@0 Coronavirus @2 NW`
C07	`01`	`X`	`SPA`	`@0 Coronavirus @2 NW`
C07	`02`	`X`	`FRE`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`ENG`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`SPA`	`@0 Coronaviridae @2 NW`
C07	`03`	`X`	`FRE`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`ENG`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`SPA`	`@0 Nidovirales @2 NW`
C07	`04`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`04`	`X`	`ENG`	`@0 Virus @2 NW`
C07	`04`	`X`	`SPA`	`@0 Virus @2 NW`
N21				`@1 171`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 05-0250654 INIST
ET :	Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus
AU :	ZHENG (Bo-Jian); YI GUAN; HE (Ming-Liang); HONGZHE SUN; LANYING DU; YING ZHENG; WONG (Kin-Ling); HONGLIN CHEN; YING CHEN; LINYU LU; TANNER (Julian A); WATT (Rory M.); NICCOLAI (Neri); BERNINI (Andrea); SPIGA (Ottavia); WOO (Patrick C. Y.); KUNG (Hsiang-Fu); YUEN (Kwok-Yung); HUANG (Jian-Dong)
AF :	Department of Microbiology, University of Hong Kong/Pokfulam/Hong-Kong (1 aut., 2 aut., 5 aut., 6 aut., 7 aut., 8 aut., 9 aut., 16 aut., 18 aut.); Institute of Molecular Biology, University of Hong Kong/Pokfulam/Hong-Kong (3 aut., 17 aut.); Centre for Emerging Infectious Diseases, Faculty of Medicine, Chinese University of Hong Kong/Hong-Kong (3 aut., 17 aut.); Department of Chemistry and Open Laboratory of Chemical Biology, University of Hong Kong/Pokfulam/Hong-Kong (4 aut., 12 aut.); Department of Biochemistry, University of Hong Kong/Pokfulam/Hong-Kong (10 aut., 11 aut., 12 aut., 19 aut.); Biomolecular Structure Research Centre, University of Siena/Siena/Italie (13 aut., 14 aut., 15 aut.)
DT :	Publication en série; Niveau analytique
SO :	Antiviral therapy : (London); ISSN 1359-6535; Royaume-Uni; Da. 2005; Vol. 10; No. 3; Pp. 393-403; Bibl. 39 ref.
LA :	Anglais
EA :	A novel severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) has been identified as the aetiological agent of SARS. We previously isolated and characterized SARS-CoV and SARS-CoV-like viruses from human and animals, respectively, suggesting that SARS could be transmitted from wild/farmed animals to humans. Comparison of the viral genomes indicated that sequence variation between animal and human isolates existed mainly in the spike (S) gene. We hypothesized that these variations may underlie a change of binding specificity of the S protein to the host cells, permitting viral transmission from animals to humans. Here we report that four 20-mer synthetic peptides (S protein fragments), designed to span these sequence variation hotspots, exhibited significant antiviral activities in a cell line. SARS-CoV infectivity was reduced over 10000-fold through pre-incubation with two of these peptides, while it was completely inhibited in the presence of three peptides. Molecular modelling of the SARS-CoV peplomer suggests that three of these antiviral peptides map to the interfaces between the three monomers of the trimeric peplomer rather than the heptad repeat region from which short peptides are known to inhibit viral entry. Our results revealed novel regions in the spike protein that can be targeted to inhibit viral infection. The peptides identified in this study could be further developed into antiviral drugs.
CC :	002B02S05
FD :	Peptide; Protéine; Virus syndrome respiratoire aigu sévère
FG :	Coronavirus; Coronaviridae; Nidovirales; Virus
ED :	Peptides; Protein; Severe acute respiratory syndrome virus
EG :	Coronavirus; Coronaviridae; Nidovirales; Virus
SD :	Péptido; Proteína; Severe acute respiratory syndrome virus
LO :	INIST-27047.354000125439640030
ID :	05-0250654

Links to Exploration step

Pascal:05-0250654

Le document en format XML

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<author><name sortKey="Spiga, Ottavia" sort="Spiga, Ottavia" uniqKey="Spiga O" first="Ottavia" last="Spiga">Ottavia Spiga</name>
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<author><name sortKey="Woo, Patrick C Y" sort="Woo, Patrick C Y" uniqKey="Woo P" first="Patrick C. Y." last="Woo">Patrick C. Y. Woo</name>
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<author><name sortKey="Kung, Hsiang Fu" sort="Kung, Hsiang Fu" uniqKey="Kung H" first="Hsiang-Fu" last="Kung">Hsiang-Fu Kung</name>
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<author><name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
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<author><name sortKey="Huang, Jian Dong" sort="Huang, Jian Dong" uniqKey="Huang J" first="Jian-Dong" last="Huang">Jian-Dong Huang</name>
<affiliation><inist:fA14 i1="05"><s1>Department of Biochemistry, University of Hong Kong</s1>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus</title>
<author><name sortKey="Zheng, Bo Jian" sort="Zheng, Bo Jian" uniqKey="Zheng B" first="Bo-Jian" last="Zheng">Bo-Jian Zheng</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
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<s3>HKG</s3>
<sZ>3 aut.</sZ>
<sZ>17 aut.</sZ>
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<sZ>3 aut.</sZ>
<sZ>17 aut.</sZ>
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<affiliation><inist:fA14 i1="04"><s1>Department of Chemistry and Open Laboratory of Chemical Biology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>4 aut.</sZ>
<sZ>12 aut.</sZ>
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<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
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<author><name sortKey="Ying Zheng" sort="Ying Zheng" uniqKey="Ying Zheng" last="Ying Zheng">YING ZHENG</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>16 aut.</sZ>
<sZ>18 aut.</sZ>
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<author><name sortKey="Wong, Kin Ling" sort="Wong, Kin Ling" uniqKey="Wong K" first="Kin-Ling" last="Wong">Kin-Ling Wong</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>16 aut.</sZ>
<sZ>18 aut.</sZ>
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<author><name sortKey="Honglin Chen" sort="Honglin Chen" uniqKey="Honglin Chen" last="Honglin Chen">HONGLIN CHEN</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>16 aut.</sZ>
<sZ>18 aut.</sZ>
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<author><name sortKey="Ying Chen" sort="Ying Chen" uniqKey="Ying Chen" last="Ying Chen">YING CHEN</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>16 aut.</sZ>
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<author><name sortKey="Linyu Lu" sort="Linyu Lu" uniqKey="Linyu Lu" last="Linyu Lu">LINYU LU</name>
<affiliation><inist:fA14 i1="05"><s1>Department of Biochemistry, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>10 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>12 aut.</sZ>
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<author><name sortKey="Tanner, Julian A" sort="Tanner, Julian A" uniqKey="Tanner J" first="Julian A" last="Tanner">Julian A. Tanner</name>
<affiliation><inist:fA14 i1="05"><s1>Department of Biochemistry, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>10 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>12 aut.</sZ>
<sZ>19 aut.</sZ>
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<author><name sortKey="Watt, Rory M" sort="Watt, Rory M" uniqKey="Watt R" first="Rory M." last="Watt">Rory M. Watt</name>
<affiliation><inist:fA14 i1="04"><s1>Department of Chemistry and Open Laboratory of Chemical Biology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>4 aut.</sZ>
<sZ>12 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="05"><s1>Department of Biochemistry, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>10 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>12 aut.</sZ>
<sZ>19 aut.</sZ>
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</affiliation>
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<author><name sortKey="Niccolai, Neri" sort="Niccolai, Neri" uniqKey="Niccolai N" first="Neri" last="Niccolai">Neri Niccolai</name>
<affiliation><inist:fA14 i1="06"><s1>Biomolecular Structure Research Centre, University of Siena</s1>
<s2>Siena</s2>
<s3>ITA</s3>
<sZ>13 aut.</sZ>
<sZ>14 aut.</sZ>
<sZ>15 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Bernini, Andrea" sort="Bernini, Andrea" uniqKey="Bernini A" first="Andrea" last="Bernini">Andrea Bernini</name>
<affiliation><inist:fA14 i1="06"><s1>Biomolecular Structure Research Centre, University of Siena</s1>
<s2>Siena</s2>
<s3>ITA</s3>
<sZ>13 aut.</sZ>
<sZ>14 aut.</sZ>
<sZ>15 aut.</sZ>
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</affiliation>
</author>
<author><name sortKey="Spiga, Ottavia" sort="Spiga, Ottavia" uniqKey="Spiga O" first="Ottavia" last="Spiga">Ottavia Spiga</name>
<affiliation><inist:fA14 i1="06"><s1>Biomolecular Structure Research Centre, University of Siena</s1>
<s2>Siena</s2>
<s3>ITA</s3>
<sZ>13 aut.</sZ>
<sZ>14 aut.</sZ>
<sZ>15 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Woo, Patrick C Y" sort="Woo, Patrick C Y" uniqKey="Woo P" first="Patrick C. Y." last="Woo">Patrick C. Y. Woo</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
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<sZ>18 aut.</sZ>
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<author><name sortKey="Kung, Hsiang Fu" sort="Kung, Hsiang Fu" uniqKey="Kung H" first="Hsiang-Fu" last="Kung">Hsiang-Fu Kung</name>
<affiliation><inist:fA14 i1="02"><s1>Institute of Molecular Biology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>3 aut.</sZ>
<sZ>17 aut.</sZ>
</inist:fA14>
</affiliation>
<affiliation><inist:fA14 i1="03"><s1>Centre for Emerging Infectious Diseases, Faculty of Medicine, Chinese University of Hong Kong</s1>
<s3>HKG</s3>
<sZ>3 aut.</sZ>
<sZ>17 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name>
<affiliation><inist:fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>16 aut.</sZ>
<sZ>18 aut.</sZ>
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</affiliation>
</author>
<author><name sortKey="Huang, Jian Dong" sort="Huang, Jian Dong" uniqKey="Huang J" first="Jian-Dong" last="Huang">Jian-Dong Huang</name>
<affiliation><inist:fA14 i1="05"><s1>Department of Biochemistry, University of Hong Kong</s1>
<s2>Pokfulam</s2>
<s3>HKG</s3>
<sZ>10 aut.</sZ>
<sZ>11 aut.</sZ>
<sZ>12 aut.</sZ>
<sZ>19 aut.</sZ>
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<series><title level="j" type="main">Antiviral therapy : (London)</title>
<title level="j" type="abbreviated">Antivir. ther. : (Lond.)</title>
<idno type="ISSN">1359-6535</idno>
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<front><div type="abstract" xml:lang="en">A novel severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) has been identified as the aetiological agent of SARS. We previously isolated and characterized SARS-CoV and SARS-CoV-like viruses from human and animals, respectively, suggesting that SARS could be transmitted from wild/farmed animals to humans. Comparison of the viral genomes indicated that sequence variation between animal and human isolates existed mainly in the spike (S) gene. We hypothesized that these variations may underlie a change of binding specificity of the S protein to the host cells, permitting viral transmission from animals to humans. Here we report that four 20-mer synthetic peptides (S protein fragments), designed to span these sequence variation hotspots, exhibited significant antiviral activities in a cell line. SARS-CoV infectivity was reduced over 10000-fold through pre-incubation with two of these peptides, while it was completely inhibited in the presence of three peptides. Molecular modelling of the SARS-CoV peplomer suggests that three of these antiviral peptides map to the interfaces between the three monomers of the trimeric peplomer rather than the heptad repeat region from which short peptides are known to inhibit viral entry. Our results revealed novel regions in the spike protein that can be targeted to inhibit viral infection. The peptides identified in this study could be further developed into antiviral drugs.</div>
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<fA11 i1="19" i2="1"><s1>HUANG (Jian-Dong)</s1>
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<fA14 i1="01"><s1>Department of Microbiology, University of Hong Kong</s1>
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<fA14 i1="03"><s1>Centre for Emerging Infectious Diseases, Faculty of Medicine, Chinese University of Hong Kong</s1>
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<sZ>17 aut.</sZ>
</fA14>
<fA14 i1="04"><s1>Department of Chemistry and Open Laboratory of Chemical Biology, University of Hong Kong</s1>
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<sZ>12 aut.</sZ>
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<server><NO>PASCAL 05-0250654 INIST</NO>
<ET>Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus</ET>
<AU>ZHENG (Bo-Jian); YI GUAN; HE (Ming-Liang); HONGZHE SUN; LANYING DU; YING ZHENG; WONG (Kin-Ling); HONGLIN CHEN; YING CHEN; LINYU LU; TANNER (Julian A); WATT (Rory M.); NICCOLAI (Neri); BERNINI (Andrea); SPIGA (Ottavia); WOO (Patrick C. Y.); KUNG (Hsiang-Fu); YUEN (Kwok-Yung); HUANG (Jian-Dong)</AU>
<AF>Department of Microbiology, University of Hong Kong/Pokfulam/Hong-Kong (1 aut., 2 aut., 5 aut., 6 aut., 7 aut., 8 aut., 9 aut., 16 aut., 18 aut.); Institute of Molecular Biology, University of Hong Kong/Pokfulam/Hong-Kong (3 aut., 17 aut.); Centre for Emerging Infectious Diseases, Faculty of Medicine, Chinese University of Hong Kong/Hong-Kong (3 aut., 17 aut.); Department of Chemistry and Open Laboratory of Chemical Biology, University of Hong Kong/Pokfulam/Hong-Kong (4 aut., 12 aut.); Department of Biochemistry, University of Hong Kong/Pokfulam/Hong-Kong (10 aut., 11 aut., 12 aut., 19 aut.); Biomolecular Structure Research Centre, University of Siena/Siena/Italie (13 aut., 14 aut., 15 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Antiviral therapy : (London); ISSN 1359-6535; Royaume-Uni; Da. 2005; Vol. 10; No. 3; Pp. 393-403; Bibl. 39 ref.</SO>
<LA>Anglais</LA>
<EA>A novel severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) has been identified as the aetiological agent of SARS. We previously isolated and characterized SARS-CoV and SARS-CoV-like viruses from human and animals, respectively, suggesting that SARS could be transmitted from wild/farmed animals to humans. Comparison of the viral genomes indicated that sequence variation between animal and human isolates existed mainly in the spike (S) gene. We hypothesized that these variations may underlie a change of binding specificity of the S protein to the host cells, permitting viral transmission from animals to humans. Here we report that four 20-mer synthetic peptides (S protein fragments), designed to span these sequence variation hotspots, exhibited significant antiviral activities in a cell line. SARS-CoV infectivity was reduced over 10000-fold through pre-incubation with two of these peptides, while it was completely inhibited in the presence of three peptides. Molecular modelling of the SARS-CoV peplomer suggests that three of these antiviral peptides map to the interfaces between the three monomers of the trimeric peplomer rather than the heptad repeat region from which short peptides are known to inhibit viral entry. Our results revealed novel regions in the spike protein that can be targeted to inhibit viral infection. The peptides identified in this study could be further developed into antiviral drugs.</EA>
<CC>002B02S05</CC>
<FD>Peptide; Protéine; Virus syndrome respiratoire aigu sévère</FD>
<FG>Coronavirus; Coronaviridae; Nidovirales; Virus</FG>
<ED>Peptides; Protein; Severe acute respiratory syndrome virus</ED>
<EG>Coronavirus; Coronaviridae; Nidovirales; Virus</EG>
<SD>Péptido; Proteína; Severe acute respiratory syndrome virus</SD>
<LO>INIST-27047.354000125439640030</LO>
<ID>05-0250654</ID>
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Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus

Synthetic peptides outside the spike protein heptad repeat regions as potent inhibitors of SARS-associated coronavirus

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