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Journal of Virology, September 2008, p. 8887-8890, Vol. 82, No. 17
0022-538X/08/$08.00+0     doi:10.1128/JVI.00415-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Cathepsin L Functionally Cleaves the Severe Acute Respiratory Syndrome Coronavirus Class I Fusion Protein Upstream of Rather than Adjacent to the Fusion Peptide{triangledown}

Berend Jan Bosch, Willem Bartelink, and Peter J. M. Rottier*

Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Faculty of Veterinary Medicine, and Institute of Biomembranes, Yalelaan 1, 3584 CL Utrecht, The Netherlands

Received 26 February 2008/ Accepted 9 June 2008

Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory sydrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.

* Corresponding author. Mailing address: Virology Division, Department of Infectious Diseases and Immunology, Utrecht University, Faculty of Veterinary Medicine, Yalelaan 1, 3584 CL Utrecht, P.O. Box 80.165, 3508 TD Utrecht, The Netherlands. Phone: 31-30-2532462. Fax: 31-30-2536723. E-mail: p.rottier{at}uu.nl

{triangledown} Published ahead of print on 18 June 2008.

Journal of Virology, September 2008, p. 8887-8890, Vol. 82, No. 17
0022-538X/08/$08.00+0     doi:10.1128/JVI.00415-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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