SARS-CoV, but not HCoV-NL63, utilizes cathepsins to infect cells: Viral entry

Advances in Experimental Medicine and Biology

Volumn 581, Issue , 2006, Pages 335-338

  Huang, I Chueh ^a   Bosch, Berend Jan ^b   Li, Wenhui ^a   Farzan, Michael ^a   Rottier, Peter M ^b   Choe, Hyeryun ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UTRECHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84934441685     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-33012-9_60     Document Type: Conference Paper

References (14)

1. C. L. Yeager, R. A. Ashmun, R. K. Williams, C. B. Cardellichio, L. H. Shapiro, S. T. Look, and K. V. Holmes, Human aminopeptidase N is a receptor for human coronavirus 229E, Nature 357:420-422 (1992).
2. D. B. Tresnan and K. V. Holmes, Feline aminopeptidase N is a receptor for all group I coronaviruses, Adv. Exp. Med. Biol. 440, 69-75 (1998).
3. W. Li, M. J. Moore, N. Vasilieva, J. Sui, S. K. Wong, M. A. Berne, M. Somasundaran, J. L. Sullivan, C. Luzeriaga, T. C. Greenough, H. Choe, and M. Farzan, Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus, Nature 426, 450-454 (2003).
4. P. Wang, J. Chen, A. Zheng, Y. Nie, X. Shi, W. Wang, G. Wang, M. Luo, H. Liu, L. Tan, X. Song, Z. Wang, X. Yin, X. Qu, X. Wang, T. Qing, M. Ding, and H. Deng, Expression cloning of functional receptor used by SARS coronavirus, Biochem. Biophys. Res. Commun. 315, 439-444 (2004).
5. H. Hofmann, K. Pyrc, L. van der Hoek, M. Geier, B. Berkhout, and S. Pohlmann, Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry, Proc. Natl. Acad. Sci. USA 16, 7988-7993 (2005).
6. S. K. Wong, W. Li, M. J. Moore, H. Choe, and M. Farzan, A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2, J. Biol. Chem. 279, 3197-3201 (2004).
7. A. Bonavia, B. D. Zelus, D. E. Wentworth, P. J. Talbot, and K. V. Holmes, Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E, J. Virol. 77, 2530-2538 (2003).
8. D. S. Dimitrov, Virus entry: molecular mechanisms and biomedical applications, Nat. Rev. Microbiol. 2, 109-122 (2004).
9. J. W. Golden, J. Linke, S. Schmechel, K. Thoemke, and L. A. Schiff, Addition of exogenous protease facilitates reovirus infection in many restrictive cells, J. Virol. 76, 7430-7443 (2002).
10. D. H. Ebert, J. Deussing, C. Peters, and T. S. Dermody, Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells, J. Biol. Chem. 277, 24609-24617 (2002).
11. J. Jane-Valbuena, L. A. Breun, L. A. Schiff, and M. L. Nibert, Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein sigma 3, J. Virol. 76, 5184-5197 (2002).
12. G. S. Baer, D. H. Ebert, C. J. Chung, A. H. Erickson, and T. S. Dermody, Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly, J. Virol. 73, 9532-9543 (1999).
13. K. Chandran, N. J. Sullivan, U. Felbor, S. P. Whelan, and J. M. Cunningham, Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection, Science 308, 1643-1645 (2005).
14. G. Simmons, J. D. Reeves, A. J. Rennekamp, S. M. Amberg, A. J. Piefer, and P. Bates, Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry, Proc. Natl. Acad. Sci. USA 101, 4240-4245 (2004).