SrasV1, PascalFrancis, Corpus, bibRecord, 000018

Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research

Identifieur interne : 000018 ( PascalFrancis/Corpus ); précédent : 000017; suivant : 000019

Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research

Auteurs : Graham Simmons ; Pawel Zmora ; Stefanie Gierer ; Adeline Heurich ; Stefan Pöhlmann

Source :

Antiviral research [ 0166-3542 ] ; 2013.

RBID : Pascal:14-0035479

Descripteurs français

Pascal (Inist)
- Activation, Virus syndrome respiratoire aigu sévère, Protéine, Enzyme, Antiviral, Relation structure activité, Syndrome respiratoire aigu sévère, Cathepsin L, Protéine S, Protéolyse, Transmembrane protease serine 2, Syndrome respiratoire du Moyen-Orient.

English descriptors

KwdEn :
- Activation, Antiviral, Cathepsin L, Enzyme, Middle East respiratory syndrome, Protein, Protein S, Proteolysis, Severe acute respiratory syndrome, Severe acute respiratory syndrome virus, Structure activity relation.

Abstract

The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses."

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A11	`03`	`1`		`@1 GIERER (Stefanie)`
A11	`04`	`1`		`@1 HEURICH (Adeline)`
A11	`05`	`1`		`@1 PÖHLMANN (Stefan)`
A14	`01`			`@1 Blood Systems Research Institute, 270 Masonic Ave @2 San Francisco, CA 94118 @3 USA @Z 1 aut.`
A14	`02`			`@1 Infection Biology Unit, German Primate Center, Kellnerweg 4 @2 37077 Göttingen @3 DEU @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut.`
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A21				`@1 2013`
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C01	`01`		`ENG`	@0 The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses."
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C03	`01`	`X`	`ENG`	`@0 Activation @5 01`
C03	`01`	`X`	`SPA`	`@0 Activación @5 01`
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C03	`06`	`X`	`SPA`	`@0 Relación estructura actividad @5 06`
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C03	`08`	`X`	`FRE`	`@0 Cathepsin L @2 FE @5 08`
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C03	`08`	`X`	`SPA`	`@0 Cathepsin L @2 FE @5 08`
C03	`09`	`X`	`FRE`	`@0 Protéine S @5 10`
C03	`09`	`X`	`ENG`	`@0 Protein S @5 10`
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C07	`05`	`X`	`ENG`	`@0 Viral disease`
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C07	`06`	`X`	`SPA`	`@0 Infección`
C07	`07`	`X`	`FRE`	`@0 Cysteine endopeptidases @2 FE`
C07	`07`	`X`	`ENG`	`@0 Cysteine endopeptidases @2 FE`
C07	`07`	`X`	`SPA`	`@0 Cysteine endopeptidases @2 FE`
C07	`08`	`X`	`FRE`	`@0 Peptidases @2 FE`
C07	`08`	`X`	`ENG`	`@0 Peptidases @2 FE`
C07	`08`	`X`	`SPA`	`@0 Peptidases @2 FE`
C07	`09`	`X`	`FRE`	`@0 Hydrolases @2 FE`
C07	`09`	`X`	`ENG`	`@0 Hydrolases @2 FE`
C07	`09`	`X`	`SPA`	`@0 Hydrolases @2 FE`
C07	`10`	`X`	`FRE`	`@0 Régulation @5 37`
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C07	`10`	`X`	`SPA`	`@0 Regulación @5 37`
C07	`11`	`X`	`FRE`	`@0 Pathologie de l'appareil respiratoire @5 38`
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N21				`@1 041`

Format Inist (serveur)

NO :	PASCAL 14-0035479 INIST
ET :	Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research
AU :	SIMMONS (Graham); ZMORA (Pawel); GIERER (Stefanie); HEURICH (Adeline); PÖHLMANN (Stefan)
AF :	Blood Systems Research Institute, 270 Masonic Ave/San Francisco, CA 94118/Etats-Unis (1 aut.); Infection Biology Unit, German Primate Center, Kellnerweg 4/37077 Göttingen/Allemagne (2 aut., 3 aut., 4 aut., 5 aut.)
DT :	Publication en série; Niveau analytique
SO :	Antiviral research; ISSN 0166-3542; Coden ARSRDR; Royaume-Uni; Da. 2013; Vol. 100; No. 3; Pp. 605-614; Bibl. 2 p.1/4
LA :	Anglais
EA :	The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses."
CC :	002B02S05; 002B05C02C
FD :	Activation; Virus syndrome respiratoire aigu sévère; Protéine; Enzyme; Antiviral; Relation structure activité; Syndrome respiratoire aigu sévère; Cathepsin L; Protéine S; Protéolyse; Transmembrane protease serine 2; Syndrome respiratoire du Moyen-Orient
FG :	Coronavirus; Coronaviridae; Nidovirales; Virus; Virose; Infection; Cysteine endopeptidases; Peptidases; Hydrolases; Régulation; Pathologie de l'appareil respiratoire; Pathologie des poumons
ED :	Activation; Severe acute respiratory syndrome virus; Protein; Enzyme; Antiviral; Structure activity relation; Severe acute respiratory syndrome; Cathepsin L; Protein S; Proteolysis; Middle East respiratory syndrome
EG :	Coronavirus; Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Cysteine endopeptidases; Peptidases; Hydrolases; Regulation(control); Respiratory disease; Lung disease
SD :	Activación; Severe acute respiratory syndrome virus; Proteína; Enzima; Antiviral; Relación estructura actividad; Síndrome respiratorio agudo severo; Cathepsin L; Proteína S; Proteolisis
LO :	INIST-18839.354000501604160040
ID :	14-0035479

Links to Exploration step

Pascal:14-0035479

Le document en format XML

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<fC02 i1="02" i2="X"><s0>002B05C02C</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Activation</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Activation</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Activación</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Virus syndrome respiratoire aigu sévère</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Severe acute respiratory syndrome virus</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Severe acute respiratory syndrome virus</s0>
<s2>NW</s2>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Protéine</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Protein</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Proteína</s0>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Antiviral</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Antiviral</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Antiviral</s0>
<s5>05</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Relation structure activité</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Structure activity relation</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Relación estructura actividad</s0>
<s5>06</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0>
<s2>NM</s2>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0>
<s2>NM</s2>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0>
<s2>NM</s2>
<s5>07</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Cathepsin L</s0>
<s2>FE</s2>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Cathepsin L</s0>
<s2>FE</s2>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Cathepsin L</s0>
<s2>FE</s2>
<s5>08</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Protéine S</s0>
<s5>10</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Protein S</s0>
<s5>10</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Proteína S</s0>
<s5>10</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Protéolyse</s0>
<s5>11</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Proteolysis</s0>
<s5>11</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Proteolisis</s0>
<s5>11</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Transmembrane protease serine 2</s0>
<s4>INC</s4>
<s5>86</s5>
</fC03>
<fC03 i1="12" i2="X" l="FRE"><s0>Syndrome respiratoire du Moyen-Orient</s0>
<s4>CD</s4>
<s5>97</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Middle East respiratory syndrome</s0>
<s4>CD</s4>
<s5>97</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Coronavirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Coronavirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Coronavirus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Virose</s0>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Viral disease</s0>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Virosis</s0>
</fC07>
<fC07 i1="06" i2="X" l="FRE"><s0>Infection</s0>
</fC07>
<fC07 i1="06" i2="X" l="ENG"><s0>Infection</s0>
</fC07>
<fC07 i1="06" i2="X" l="SPA"><s0>Infección</s0>
</fC07>
<fC07 i1="07" i2="X" l="FRE"><s0>Cysteine endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="07" i2="X" l="ENG"><s0>Cysteine endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="07" i2="X" l="SPA"><s0>Cysteine endopeptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="08" i2="X" l="FRE"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="08" i2="X" l="ENG"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="08" i2="X" l="SPA"><s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="09" i2="X" l="FRE"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="09" i2="X" l="ENG"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="09" i2="X" l="SPA"><s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="10" i2="X" l="FRE"><s0>Régulation</s0>
<s5>37</s5>
</fC07>
<fC07 i1="10" i2="X" l="ENG"><s0>Regulation(control)</s0>
<s5>37</s5>
</fC07>
<fC07 i1="10" i2="X" l="SPA"><s0>Regulación</s0>
<s5>37</s5>
</fC07>
<fC07 i1="11" i2="X" l="FRE"><s0>Pathologie de l'appareil respiratoire</s0>
<s5>38</s5>
</fC07>
<fC07 i1="11" i2="X" l="ENG"><s0>Respiratory disease</s0>
<s5>38</s5>
</fC07>
<fC07 i1="11" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0>
<s5>38</s5>
</fC07>
<fC07 i1="12" i2="X" l="FRE"><s0>Pathologie des poumons</s0>
<s5>39</s5>
</fC07>
<fC07 i1="12" i2="X" l="ENG"><s0>Lung disease</s0>
<s5>39</s5>
</fC07>
<fC07 i1="12" i2="X" l="SPA"><s0>Pulmón patología</s0>
<s5>39</s5>
</fC07>
<fN21><s1>041</s1>
</fN21>
</pA>
</standard>
<server><NO>PASCAL 14-0035479 INIST</NO>
<ET>Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research</ET>
<AU>SIMMONS (Graham); ZMORA (Pawel); GIERER (Stefanie); HEURICH (Adeline); PÖHLMANN (Stefan)</AU>
<AF>Blood Systems Research Institute, 270 Masonic Ave/San Francisco, CA 94118/Etats-Unis (1 aut.); Infection Biology Unit, German Primate Center, Kellnerweg 4/37077 Göttingen/Allemagne (2 aut., 3 aut., 4 aut., 5 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Antiviral research; ISSN 0166-3542; Coden ARSRDR; Royaume-Uni; Da. 2013; Vol. 100; No. 3; Pp. 605-614; Bibl. 2 p.1/4</SO>
<LA>Anglais</LA>
<EA>The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses."</EA>
<CC>002B02S05; 002B05C02C</CC>
<FD>Activation; Virus syndrome respiratoire aigu sévère; Protéine; Enzyme; Antiviral; Relation structure activité; Syndrome respiratoire aigu sévère; Cathepsin L; Protéine S; Protéolyse; Transmembrane protease serine 2; Syndrome respiratoire du Moyen-Orient</FD>
<FG>Coronavirus; Coronaviridae; Nidovirales; Virus; Virose; Infection; Cysteine endopeptidases; Peptidases; Hydrolases; Régulation; Pathologie de l'appareil respiratoire; Pathologie des poumons</FG>
<ED>Activation; Severe acute respiratory syndrome virus; Protein; Enzyme; Antiviral; Structure activity relation; Severe acute respiratory syndrome; Cathepsin L; Protein S; Proteolysis; Middle East respiratory syndrome</ED>
<EG>Coronavirus; Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Cysteine endopeptidases; Peptidases; Hydrolases; Regulation(control); Respiratory disease; Lung disease</EG>
<SD>Activación; Severe acute respiratory syndrome virus; Proteína; Enzima; Antiviral; Relación estructura actividad; Síndrome respiratorio agudo severo; Cathepsin L; Proteína S; Proteolisis</SD>
<LO>INIST-18839.354000501604160040</LO>
<ID>14-0035479</ID>
</server>
</inist>
</record>

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Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research

Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research

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