Figure 1 (Top) Diagram of the three different particles; (Bottom) Negative contrast electron micrograph of particles of Cowpea mosaic virus (genus Comovirus). The bar represents 50 nm.
Figure 2 Architecture of the capsids of a picornavirus (top), a comovirus (middle) and a nepovirus (bottom).
Figure 3 Organization and expression of the genome of Cowpea mosaic virus (CPMV). The positions of the start and stop codons are indicated on the RNA, and functions of the proteins are indicated in the ORF of the RNA. MP, movement protein; L, large capsid protein; S, small capsid protein; C-Pro, processing regulator: NTP, nucleotide binding protein; Pro, proteinase; Pol, polymerase. Proteolytic cleavage sites are indicated on the polyproteins. All intermediate and final cleavage products have been detected in infected cells.
Figure 4 Organization and expression of the Patchouli mild mosaic virus (PatMMV) RNA-2. The position of the start and stop codon are indicated on the RNA, and functions of the proteins are indicated in the ORF of the RNA. MP?, putative MP; L, large CP; S, small CP. Proteolytic cleavage sites are indicated on the polyprotein.
Figure 5 Organization and expression of the genome of Beet ringspot virus (BRSV). The positions of the start and stop codons are indicated on the RNA, and functions of the proteins are indicated in the ORF of the RNA. MP, movement protein; CP, capsid protein; NTP, nucleotide binding protein; PRO, proteinase; POL, polymerase. Proteolytic cleavage sites are indicated on the polyproteins.
Figure 6 Phylogenetic tree derived from the alignment of the polymerase protein sequences of virus species belonging to the family Comoviridae using the Clustal method. The horizontal scale is proportional to the percentage of divergence while the vertical scale is arbitrary.
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