A multiple alignment of the capsid protein sequences of nepoviruses and comoviruses suggests a common structure.
The amino acid sequences of the regions encoding the structural proteins of eleven nepoviruses and five comoviruses, two genera of the family Comoviridae, have been aligned. The properties predicted by computer analysis (three-dimensional-3D-structure, hydrophobicity) are also correlated along this alignment, and aligned to the experimentally determined 3D structure of two comoviruses. It can thus be assumed that the 3D structure of the unique nepovirus coat protein matches that of the bipartite protomer found in the comovirus particles. In this model, the spatial locations of two amino-acid motifs characteristic of nepoviruses are in close vicinity, at the external surface of the virion. The coat proteins of nepoviruses and comoviruses may thus share a common evolutionary origin. A phylogenetic analysis was made using the multiple alignment, allowing a better understanding of the molecular relationships between these two groups of viruses.
Le Gall
O
O
Station de Pathologie Végétale, INRA, Villenave d'Ornon, France.
Candresse
T
T
Dunez
J
J
D000595:Amino Acid Sequence; D001483:Base Sequence; D002213:Capsid / Q000737:chemistry* / Q000235:genetics; D017798:Comovirus / Q000145:classification*; D008969:Molecular Sequence Data; D017860:Nepovirus / Q000145:classification*; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012995:Solubility