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Modification of the trypsin cleavage site of rotavirus VP4 to a furin-sensitive form does not enhance replication efficiency
Modification of the trypsin cleavage site of rotavirus VP4 to a furin-sensitive form does not enhance replication efficiency
- Source :
- The Journal of general virology. 92(Pt 12)
- Publication Year :
- 2011
-
Abstract
- The infectivity of rotavirus (RV) is dependent on an activation process triggered by the proteolytic cleavage of its spike protein VP4. This activation cleavage is performed by exogenous trypsin in the lumen of the intestinesin vivo. Here, we report the generation and characterization of a recombinant RV expressing cDNA-derived VP4 with a modified cleavage site (arginine at position 247) recognized by endogenous furin as well as exogenous trypsin. Unexpectedly, the mutant virus (KU//rVP4-R247Furin) was incapable of plaque formation without an exogenous protease, although the mutant VP4s on virions were efficiently cleaved by endogenous furin. Furthermore, KU//rVP4-R247Furin showed impaired infectivity in MA104 and CV-1 cells even in the presence of trypsin compared with the parental virus carrying authentic VP4 (KU//rVP4). Although the total titre of KU//rVP4-R247Furin was comparable to that of KU//rVP4, the extracellular titre of KU//rVP4-R247Furin was markedly lower than its cell-associated titre in comparison with that of KU//rVP4. In contrast, the two viruses showed similar growth in a furin-defective LoVo cell line. These results suggest that intracellular cleavage of VP4 by furin may be disadvantageous for RV infectivity, possibly due to an inefficient virus release process.
- Subjects :
- Gene Expression Regulation, Viral
Rotavirus
viruses
medicine.medical_treatment
Blotting, Western
Viral Plaque Assay
Biology
Cleavage (embryo)
Virus Replication
Virus
Cell Line
Virology
Chlorocebus aethiops
medicine
Animals
Trypsin
DNA Cleavage
Furin
Infectivity
Protease
Virion
Molecular biology
Viral replication
Cell culture
COS Cells
Mutation
biology.protein
Capsid Proteins
medicine.drug
Subjects
Details
- ISSN :
- 14652099
- Volume :
- 92
- Issue :
- Pt 12
- Database :
- OpenAIRE
- Journal :
- The Journal of general virology
- Accession number :
- edsair.doi.dedup.....5ee18255418ce04f42e21cedb661490f