2012
DOI: 10.1016/j.bbrc.2012.09.020
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Novel ATPase activity of the polyprotein intermediate, Viral Protein genome-linked-Nuclear Inclusion-a protease, of Pepper vein banding potyvirus

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Cited by 12 publications
(14 citation statements)
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“…The slow release of VPg from the NIa fusion, consisting of the Nterminal VPg domain and the C-terminal NIa-Pro protease domain, is required for the infectivity of the Tobacco etch virus (TEV; genus Potyvirus) (Schaad et al, 1996). Furthermore, the interaction of the VPg domain with the NIa-Pro domain increases the protease turnover in Pepper vein banding virus (PVBV; genus Potyvirus) (Mathur et al, 2012). The VPg-mediated structural and functional modulation of NIa-Pro may, therefore, regulate viral proteolytic activity at particular stages of the virus life cycle.…”
Section: Regulation Of Potyviral Protein Amounts and Functionsmentioning
confidence: 99%
“…The slow release of VPg from the NIa fusion, consisting of the Nterminal VPg domain and the C-terminal NIa-Pro protease domain, is required for the infectivity of the Tobacco etch virus (TEV; genus Potyvirus) (Schaad et al, 1996). Furthermore, the interaction of the VPg domain with the NIa-Pro domain increases the protease turnover in Pepper vein banding virus (PVBV; genus Potyvirus) (Mathur et al, 2012). The VPg-mediated structural and functional modulation of NIa-Pro may, therefore, regulate viral proteolytic activity at particular stages of the virus life cycle.…”
Section: Regulation Of Potyviral Protein Amounts and Functionsmentioning
confidence: 99%
“…Competition in binding the initiation factor eIF4E or degradation of plant mRNAs by VPg ribonuclease activity may interfere with and hinder the host proteosynthesis (Grzela et al, 2006;Cotton et al, 2006). ATPase activity of the VpG has been recently demonstrated and presented in connection with its potential functions, particularly with cell-to-cell or long distance movement of potyviruses (Mathur and Savithri, 2012).…”
Section: Expression Strategy and Non-structural Proteinsmentioning
confidence: 99%
“…It has been demonstrated that the interaction of Sesbania mosaic virus (SeMV) protease with VPg in cis-(Protease-VPg) leads to the activation of the protease (Satheshkumar et al, 2005). Similarly VPg covalently linked to the N-terminus of pepper vein banding virus (PVBV) protease NIaPro (VPg-NIaPro) results in the enhancement of activity (Mathur & Savithri, 2012). In both these cases, the interaction of the disordered VPg domain alters the structure and function of the interacting proteases.…”
Section: Viral Proteasesmentioning
confidence: 99%