Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research
Identifieur interne : 000969 ( PascalFrancis/Curation ); précédent : 000968; suivant : 000970Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research
Auteurs : Graham Simmons [États-Unis] ; Pawel Zmora [Allemagne] ; Stefanie Gierer [Allemagne] ; Adeline Heurich [Allemagne] ; Stefan Pöhlmann [Allemagne]Source :
- Antiviral research [ 0166-3542 ] ; 2013.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Enzyme.
English descriptors
- KwdEn :
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."
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<fC03 i1="08" i2="X" l="ENG"><s0>Cathepsin L</s0>
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<s2>FE</s2>
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<s2>FE</s2>
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<s2>FE</s2>
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<fC07 i1="12" i2="X" l="SPA"><s0>Pulmón patología</s0>
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