Short communicationEffects of site-directed mutagenesis on the presumed catalytic triad and substrate-binding pocket of grapevine fanleaf nepovirus 24-kDa proteinase
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A Renaissance in Nepovirus Research Provides New Insights Into Their Molecular Interface With Hosts and Vectors
2017, Advances in Virus ResearchCitation Excerpt :Proteases of subgroup A and B nepoviruses recognize even more diverse cleavage sites that include cysteine, alanine, arginine, glycine, or lysine residues at the − 1 position (i.e., K/A, K/S, R/S, R/A, R/G, C/A, C/S, C/G, A/S, G/V, and G/A; Hemmer et al., 1995; Margis et al., 1993; Wetzel et al., 2008; and references therein). The divergent cleavage site specificity of subgroup A and B nepovirus Pros has been attributed to the replacement of the substrate-binding pocket histidine by a leucine (Gorbalenya and Snijder, 1996; Margis and Pinck, 1992). In addition to the residue at the − 1 position of the cleavage site, other factors influence the specificity of 3C-Pros, including the aa sequence surrounding the cleavage sites (often in positions − 6 to + 2) and the secondary structure of the polyprotein, with cleavage sites normally located in exposed loops (Ypma-Wong et al., 1988; Zunszain et al., 2010).
Characterization of a putative novel nepovirus from Aeonium sp.
2013, Virus ResearchIn vitro and in vivo evidence for differences in the protease activity of two arabis mosaic nepovirus isolates and their impact on the infectivity of chimeric cDNA clones
2013, VirologyCitation Excerpt :A conserved histidine and threonine (His161 and Thr142, in the case of poliovirus) as well as surrounding amino acids (Gly163, Gly164, Gly145, Gln146) interact with the conserved glutamine at the P1 position of the cleavage site. In the case of nepoviruses of subgroup A and B, the absence of a glutamine at the P1 position of cleavage sites is correlated with the replacement of the histidine in the substrate-binding pocket of the protease by a leucine (Gorbalenya et al., 1989; Gorbalenya and Snijder, 1996; Margis and Pinck, 1992; Ryan and Flint, 1997). An equivalent to Thr142 is not found in the sequence of subgroup A and B nepovirus proteases.
Grapevine Fanleaf Nepovirus Cysteine Proteinase
2013, Handbook of Proteolytic Enzymes