Disease relevance of Potexvirus

• The organization of potato virus X coat proteins in virus particles studied by tritium planigraphy and model building [1].
• Phylogenetic analysis based upon the amino acid sequence of the viral capsid protein also indicates that the garlic viruses have a unique and distinct domain different from those of the potexvirus and carlavirus groups [2].
• We have used an Escherichia coli expression system to produce significant amounts of the 26-kDa protein (p26) encoded by foxtail mosaic potexvirus ORF2. p28 was purified to near homogeneity by conventional purification methods and some of its biochemical properties were determined [3].
• To investigate the molecular role of the tobacco mosaic tobamovirus (TMV) coat protein (CP) in conferring cross-protection, a potato X potexvirus (PVX) vector (S. Chapman, Plant J. 2, 549-557, 1992) was used to systemically express a set of TMV mutant CPs in Nicotiana benthamiana prior to challenge inoculation with TMV [4].
• Three SAH hydrolase inhibitors, (RS)-3-adenin-9-yl-2-hydroxypropanoic acid (isobutyl ester) [(RS)-AHPA]; (RS)-9-(2,3-dihydroxypropyl)adenine [(RS)-DHPA] and the carbocyclic analog of 3-deazaadenosine (C-c3Ado) were evaluated for their inhibitory activity against tobacco mosaic virus (TMV) and potato virus X (PVX) [5].

High impact information on Potexvirus

• The contribution of individual genes was determined by bioassays with an infectious clone of wild-type TBSV, with p19/p22 mutant derivatives, and by expression of individual TBSV genes from a heterologous potato virus X (PVX) vector [6].
• Use of a gene expression system based on potato virus X to rapidly identify and characterize a tomato Pto homolog that controls fenthion sensitivity [7].
• An RNA-dependent RNA polymerase prevents meristem invasion by potato virus X and is required for the activity but not the production of a systemic silencing signal [8].
• Recently we have reported that a selective binding of potato virus X (PVX)-coded movement protein (termed TGBp1 MP) to one end of a polar coat protein (CP) helix converted viral RNA into a translatable form and induced a linear destabilization of the whole helical particle [9].
• When expressed from potato virus X, C2-RRRR(31)DVGG (in which the four consecutive arginine residues (28)RRRR(31) were replaced with DVGG) that had been tagged with a green fluorescent protein (GFP) failed to transport GFP into nuclei and was dysfunctional in inducing necrosis and suppressing PTGS in plants [10].

Chemical compound and disease context of Potexvirus

• The highly conserved ELDKWA epitope from glycoprotein (gp) 41 was expressed as an N-terminal translational fusion with the potato virus X (PVX) coat protein [11].
• The secondary structure of a 170 nt transcript derived from a cDNA clone containing the 3' untranslated region of bamboo mosaic potexvirus (BaMV) with 32 adenine residues of the poly(A) tail, was investigated in solution by using enzymatic and chemical probes [12].
• The topography of the surface of potato virus X: tritium planigraphy and immunological analysis [13].
• Less KCl (0-08 to 0-24 M) also favoured aphid transmission of PLO-treated potato virus X and tobacco rattle virus [14].
• A potato virus X (PVX) vector was used to express a single chain antibody fragment (scFv) against the herbicide diuron, as a fusion to the viral coat protein [15].

Biological context of Potexvirus

• Open reading frame 1 (ORF1) of potexviruses encodes a viral replicase comprising three functional domains: a capping enzyme at the N terminus, a putative helicase in the middle, and a polymerase at the C terminus [16].
• When compared to potex-, carla-, clostero- and capilloviruses, the ASPV genome organization appeared to be most closely related to that of potexviruses, but with a larger coat protein of M(r) 44K (ORF5) [17].
• The complete nucleotide sequence of the triple gene block one (TGB 1) of cymbidium mosaic potexvirus (CymMV) was compared to those from other potex-, carla-, furo- and hordeiviruses [18].

Anatomical context of Potexvirus

• In the present study, we tested the hypothesis that the expression levels of recombinant hGAD65 in transgenic plants can be increased by targeting the enzyme to the plant cell cytosol and by mediating expression through the potato virus X (PVX) vector [19].

Gene context of Potexvirus

• The ORF1 protein was found to be highly homologous to the putative potexvirus RNA replicases; ORF2, -3, -5 and -6 proteins also have analogues among the potex- and/or carlavirus-encoded proteins [20].
• Similar to other potexviruses, its genome organisation is comprised of five major open reading frames (ORFs 1 to 5), encoding a Mr 160 KDa putative RNA-dependent RNA polymerase (RdRp); a Mr 26KDa/13KDa/10KDa triple-gene-block (TGB) and a Mr 24 KDa coat protein [21].
• ORF5 potentially encodes a 229 aa protein of 25 kDa that is similar to the coat proteins of other potexviruses [22].
• Complementation of movement-deficient potato virus X (PVX) coat protein (CP) mutants, namely PVX.CP-Xho lacking the 18 C-terminal amino acid residues and PVX.DeltaCP lacking the entire CP gene, was studied by transient co-expression with heterologous proteins [23].
• The full sequence of the phlox isolate was more closely related to PapMV throughout the genome than to any potexvirus other than AltMV-Au, for which only the CP and 3'UTR sequences are available [24].

References