Abstract:
:Arabis mosaic virus is a subgroup A nepovirus. The RNA1-encoded polyprotein (P1) contains the domains for the NTP-binding protein (NTB), VPg, proteinase (Pro) and polymerase at its C-terminus. Putative cleavage sites delineating these domains have been proposed. However, the number and location of cleavage sites upstream of the NTB domain are not known. Using in vitro processing assays, we have confirmed proteolytic cleavage at the NTB-VPg and VPg-Pro sites. In addition, we have identified two cleavage sites in the N-terminal region of P1. Site-directed mutagenesis and immunoprecipitation experiments using inserted peptide tags confirmed that the position of these cleavage sites corresponds to that of cleavage sites delineating the X1 and X2 domains in Tomato ringspot virus (subgroup C nepovirus). Amino acid alignments implied the presence of similar cleavage sites in the P1 polyprotein of other nepoviruses. Our results suggest that the presence of two protein domains upstream of NTB is a common feature of nepoviruses.
journal_name
Virologyjournal_title
Virologyauthors
Wetzel T,Chisholm J,Bassler A,Sanfaçon Hdoi
10.1016/j.virol.2008.01.046subject
Has Abstractpub_date
2008-05-25 00:00:00pages
159-69issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(08)00081-0journal_volume
375pub_type
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