Cleavage of spike protein of SARS coronavirus by protease factor Xa is associated with viral infectivity
- Department of Microbiology, The University of Hong Kong (Hong Kong)
- State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071 (China)
- Lindsley F. Kimball Research Institute, The New York Blood Center, New York, NY 10021 (United States)
- Department of Biochemistry, The University of Hong Kong (Hong Kong)
The spike (S) protein of SARS coronavirus (SARS-CoV) has been known to recognize and bind to host receptors, whose conformational changes then facilitate fusion between the viral envelope and host cell membrane, leading to viral entry into target cells. However, other functions of SARS-CoV S protein such as proteolytic cleavage and its implications to viral infection are incompletely understood. In this study, we demonstrated that the infection of SARS-CoV and a pseudovirus bearing the S protein of SARS-CoV was inhibited by a protease inhibitor Ben-HCl. Also, the protease Factor Xa, a target of Ben-HCl abundantly expressed in infected cells, was able to cleave the recombinant and pseudoviral S protein into S1 and S2 subunits, and the cleavage was inhibited by Ben-HCl. Furthermore, this cleavage correlated with the infectivity of the pseudovirus. Taken together, our study suggests a plausible mechanism by which SARS-CoV cleaves its S protein to facilitate viral infection.
- OSTI ID:
- 20991450
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 359, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2007.05.092; PII: S0006-291X(07)01058-3; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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