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J. Biol. Chem., Vol. 277, Issue 27, 24609-24617, July 5, 2002
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From the Departments of After attachment to receptors, reovirus virions
are internalized by endocytosis and exposed to
acid-dependent proteases that catalyze viral disassembly.
Previous studies using the cysteine protease inhibitor E64 and a mutant
cell line that does not support reovirus disassembly suggest a
requirement for specific endocytic proteases in reovirus entry. This
study identifies the endocytic proteases that mediate reovirus
disassembly in murine fibroblast cells. Infection of both L929 cells
treated with the cathepsin L inhibitor
Z-Phe-Tyr(t-Bu)-diazomethyl ketone and cathepsin
L-deficient mouse embryo fibroblasts resulted in inefficient
proteolytic disassembly of viral outer-capsid proteins and decreased
viral yields. In contrast, both L929 cells treated with the cathepsin B
inhibitor CA-074Me and cathepsin B-deficient mouse embryo fibroblasts
support reovirus disassembly and growth. However, removal of both
cathepsin B and cathepsin L activity completely abrogates disassembly
and growth of reovirus. Concordantly, cathepsin L mediates reovirus disassembly more efficiently than cathepsin B in vitro.
These results demonstrate that either cathepsin L or cathepsin B is required for reovirus entry into murine fibroblasts and indicate that
cathepsin L is the primary mediator of reovirus disassembly. Moreover,
these findings suggest that specific endocytic proteases can determine
host cell susceptibility to infection by intracellular pathogens.
Cathepsin L and Cathepsin B Mediate Reovirus Disassembly in
Murine Fibroblast Cells*
§,
,§**
Microbiology and Immunology
and ** Pediatrics and § Elizabeth B. Lamb Center
for Pediatric Research, Vanderbilt University School of Medicine,
Nashville, Tennessee 37232 and ¶ Institut für Molekulare
Medizin und Zellforschung, Albert-Ludwigs-Universität Freiburg,
Hugstetter Strasse 55, Freiburg, 79106 Freiburg, Federal Republic of Germany
*
This work was supported by NIGMS, National Institutes of
Health (NIH) Public Health Service Grant T32 GM07347 for the
Vanderbilt Medical Scientist Training Program (to D. H. E.), NIAID,
NIH Public Health Service Grant R01 AI32539, and the Elizabeth B. Lamb
Center for Pediatric Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Max-Planck-Institut für Psychiatrie,
Molekulare Neurogenetik, Kraepelinstrasse 2-10, 80804 München, FRG.
To whom correspondence should be addressed: Lamb Center for
Pediatric Research, D7235 MCN, Vanderbilt University School of Medicine, Nashville, TN 37232. Tel.: 615-343-9943; Fax: 615-343-9723; E-mail: terry.dermody@mcmail.vanderbilt.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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