. 2006;581:335–338. doi:10.1007/978-0-387-33012-9_60
SARS-CoV, But not HCoV-NL63, Utilizes Cathepsins to Infect Cells: Viral Entry
I-Chueh Huang3,Berend Jan Bosch4,Wenhui Li5,Michael Farzan6,Peter M Rottier7,Hyeryun Choe8
Wenhui Li
5New England Primate Research Center, 01772 Southborough, Massachusetts USA
Find articles byWenhui Li
Michael Farzan
6New England Primate Research Center, 01772 Southborough, Massachusetts USA
Find articles byMichael Farzan
Editors:Stanley Perlman1,Kathryn V Holmes2
1Department of Pediatrics, University of Iowa, 52242 Iowa City, IA USA
2Department of Microbiology, University of Colorado Health Sciences Center at Fitzsimons, 80045-8333 Aurora, CO USA
3Harvard Medical School, Boston, Massachusetts USA
4Utrecht University, Utrecht The Netherlands
5New England Primate Research Center, 01772 Southborough, Massachusetts USA
6New England Primate Research Center, 01772 Southborough, Massachusetts USA
7Utrecht University, Utrecht The Netherlands
8Harvard Medical School, Boston, Massachusetts USA
Keywords: Pseudotyped Virus, Marburg Virus, Human Coronavirus, Severe Acute Respiratory Syndrome Coronavirus, Reovirus Infection
© Springer Science+Business Media, LLC 2006
This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
PMCID: PMC7123842 PMID:17037556
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Contributor Information
Stanley Perlman, Email: Stanley-Perlman@uiowa.edu
Kathryn V. Holmes, Email: Kathryn.Holmes@ucHSC.edu
References
- 1.Yeager CL, Ashmun RA, Williams RK, Cardellichio CB, Shapiro LH, Look ST, Holmes KV. Human aminopeptidase N is a receptor for human coronavirus 229E. Nature. 1992;357:420–422. doi: 10.1038/357420a0. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 2.Tresnan DB, Holmes KV. Feline aminopeptidase N is a receptor for all group I coronaviruses. Adv. Exp. Med. Biol. 1998;440:69–75. doi: 10.1007/978-1-4615-5331-1_9. [DOI] [PubMed] [Google Scholar]
- 3.Li W, Moore MJ, Vasilieva N, Sui J, Wong SK, Berne MA, Somasundaran M, Sullivan JL, Luzeriaga C, Greenough TC, Choe H, Farzan M. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003;426:450–454. doi: 10.1038/nature02145. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 4.Wang P, Chen J, Zheng A, Nie Y, Shi X, Wang W, Wang G, Luo M, Liu H, Tan L, Song X, Wang Z, Yin X, Qu X, Wang X, Qing T, Ding M, Deng H. Expression cloning of functional receptor used by SARS coronavirus. Biochem. Biophys. Res. Commun. 2004;315:439–444. doi: 10.1016/j.bbrc.2004.01.076. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 5.Hofmann H, Pyrc K, van der Hoek L, Geier M, Berkhout B, Pohlmann S. Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry. Proc. Natl. Acad. Sci. USA. 2005;16:7988–7993. doi: 10.1073/pnas.0409465102. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 6.Wong SK, Li W, Moore MJ, Choe H, Farzan M. A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2. J. Biol. Chem. 2004;279:3197–3201. doi: 10.1074/jbc.C300520200. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 7.Bonavia A, Zelus BD, Wentworth DE, Talbot PJ, Holmes KV. Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E. J. Virol. 2003;77:2530–2538. doi: 10.1128/JVI.77.4.2530-2538.2003. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 8.Dimitrov DS. Virus entry: molecular mechanisms and biomedical applications. Nat. Rev. Microbiol. 2004;2:109–122. doi: 10.1038/nrmicro817. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 9.Golden JW, Linke J, Schmechel S, Thoemke K, Schiff LA. Addition of exogenous protease facilitates reovirus infection in many restrictive cells. J. Virol. 2002;76:7430–7443. doi: 10.1128/JVI.76.15.7430-7443.2002. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 10.Ebert DH, Deussing J, Peters C, Dermody TS. Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J. Biol. Chem. 2002;277:24609–24617. doi: 10.1074/jbc.M201107200. [DOI] [PubMed] [Google Scholar]
- 11.Jane-Valbuena J, Breun LA, Schiff LA, Nibert ML. Sites and determinants of early cleavages in the proteolytic processing pathway of reovirus surface protein sigma 3. J. Virol. 2002;76:5184–5197. doi: 10.1128/JVI.76.10.5184-5197.2002. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 12.Baer GS, Ebert DH, Chung CJ, Erickson AH, Dermody TS. Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly. J. Virol. 1999;73:9532–9543. doi: 10.1128/jvi.73.11.9532-9543.1999. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 13.Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science. 2005;308:1643–1645. doi: 10.1126/science.1110656. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 14.Simmons G, Reeves JD, Rennekamp AJ, Amberg SM, Piefer AJ, Bates P. Inhibitors of cathepsin L prevent severe acute respiratory syndrome coronavirus entry. Proc. Natl. Acad. Sci. USA. 2004;101:4240–4245. doi: 10.1073/pnas.0306446101. [DOI] [PMC free article] [PubMed] [Google Scholar]