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Tripeptidyl peptidase II serves as an alternative to impaired proteasome to maintain viral growth in the host cells
- Source :
- Febs Letters
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
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Abstract
- The ubiquitin–proteasome system is known to be utilized by coxsackievirus to facilitate its propagation within the host cells. The present study explores the role of tripeptidyl peptidase II (TPPII), a serine peptidase contributing to protein turnover by acting downstream of the proteasome, in regulating coxsackievirus infection. Inhibition of TPPII does not affect virus replication in cells with functional proteasome. However, when the proteasome is impaired, TPPII appears to serve as an alternative to maintain low levels of virus infection. Our results suggest an important function of TPPII in the maintenance of viral growth and may have implications for anti-viral therapy.
- Subjects :
- Virus replication
Leupeptins
viruses
UPS
Biochemistry
Aminopeptidases
Structural Biology
Enzyme Inhibitors
PBS
Coxsackievirus B3
Tripeptidyl peptidase II
Serine Endopeptidases
Drug Synergism
Dulbecco's modified Eagle's medium
Cell biology
Enterovirus B, Human
Host-Pathogen Interactions
H-Ala-Ala-Phe-chloromethylketone
TPPII
Proteasome Inhibitors
H-Ala-Ala-Phe-7-amino-4-methylcoumarin
Proteasome Endopeptidase Complex
Short Communication
Blotting, Western
Biophysics
Short Communications
DMEM
Biology
Coxsackievirus
Virus
H-AAF-AMC
Genetics
Humans
H-AAF-CMK
Ubiquitin/proteasome system
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
CVB3
Molecular Biology
phosphate buffered saline
Dose-Response Relationship, Drug
Host (biology)
Protein turnover
Cell Biology
biology.organism_classification
Acetylcysteine
Proteasome
Viral replication
Function (biology)
HeLa Cells
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....c275c6adb1993b66052f8a970ab37e7a
- Full Text :
- https://doi.org/10.1016/j.febslet.2010.11.056