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Título

Autoproteolytic activity derived from the infectious bursal disease virus capsid protein

Autor Irigoyen, Nerea; Garriga, Damià; Navarro, Aitor; Verdaguer, Núria ; Rodríguez, José Francisco; Castón, José R.
Palabras clave Viral protease
Virus-like particles
Viral genome
Viral capsids
Reverse genetics
Proteolytic processing
Protective shell
Pentamers
Mutant proteins
Infectious bursal disease virus
Host cells
Hexamers
Genome packaging
Enzymatic activities
Double-stranded RNA
Conformational change
Cleavage reaction
Catalytic sites
Capsid proteins
C-terminal regions
Building block
Three-dimensional structure
Fecha de publicación 19-ene-2009
EditorAmerican Society for Biochemistry and Molecular Biology
Citación Journal of Biological Chemistry 284(12): 8064-8072 (2009)
ResumenViral capsids are envisioned as vehicles to deliver the viral genome to the host cell. They are nonetheless dynamic protective shells, as they participate in numerous processes of the virus cycle such as assembly, genome packaging, binding to receptors, and uncoating among others. In so doing, they undergo large scale conformational changes. Capsid proteins with essential enzymatic activities are being described more frequently. Here we show that the precursor (pVP2) of the capsid protein VP2 of the infectious bursal disease virus (IBDV), an avian double-stranded RNA virus, has autoproteolytic activity. The pVP2 C-terminal region is first processed by the viral protease VP4. VP2 Asp-431, lying in a flexible loop preceding the C-terminal most α-helix, is responsible for the endopeptidase activity that cleaves the Ala-441-Phe-442 bond to generate the mature VP2 polypeptide. The D431N substitution abrogates the endopeptidase activity without introducing a significant conformational change, as deduced from the three-dimensional structure of the mutant protein at 3.1 riA resolution. Combinations of VP2 polypeptides containing mutations affecting either the cleavage or the catalytic site revealed that pVP2 proteolytic processing is the result of a monomolecular cis-cleavage reaction. The D431N mutation does not affect the assembly of the VP2 trimers that constitute the capsid building block. Although VP2 D431N trimers are capable of assembling both pentamers and hexamers, expression of a polyprotein gene harboring the D431N mutation does not result in the assembly of IBDV virus-like particles. Reverse genetics analyses demonstrate that pVP2 self-processing is essential for the assembly of an infectious IBDV progeny. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M808942200
URI http://hdl.handle.net/10261/110111
DOI10.1074/jbc.M808942200
Identificadoresdoi: 10.1074/jbc.M808942200
issn: 0021-9258
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