title: Analysis of a three-dimensional structure of Potato leafroll virus coat protein obtained by homology modeling.
abstract: Viruses of the family Luteoviridae are ssRNA plant viruses that have particles that exhibit icosahedral symmetry. To identify the residues that might be exposed on the surface of the Potato leafroll virus (PLRV; genus Polerovirus, family Luteoviridae) capsid, and therefore involved in biological interactions, we performed a structural analysis of the PLRV coat protein (CP) on the basis of comparisons with protein sequences and known crystal structures of CPs of other viruses. The CP of PLRV displays 33% sequence similarity with that of Rice yellow mottle virus (genus Sobemovirus) when the sequences were aligned by using the hidden Markov model method. A structure model for PLRV CP was designed by protein homology modeling, using the crystal structure of RYMV as a template. The resulting model is consistent with immunological and site-directed mutagenesis data previously reported. On the basis of this model it is possible to predict some surface properties of the PLRV CP and also speculate about the structural evolution of small icosahedral viruses.
authors.affiliation: Institut National de la Recherche Agronomique, Station de Pathologie Végétale, Le Rheu Cédex, 35653, France. terradot@biochem.wustl.edu
authors.forename: L
authors.initials: L
authors.lastname: Terradot
authors.forename: M
authors.initials: M
authors.lastname: Souchet
authors.forename: V
authors.initials: V
authors.lastname: Tran
authors.forename: D
authors.initials: D
authors.lastname: Giblot Ducray-Bourdin
mesh_terms: D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010942:Plant Viruses / Q000737:chemistry*; D011487:Protein Conformation; D016415:Sequence Alignment; D011198:Solanum tuberosum / Q000821:virology*