title: Tomato yellow leaf curl virus (TYLCV) capsid protein (CP) subunit interactions: implications for viral assembly.
abstract: Tomato yellow leaf curl virus (TYLCV) capsid protein (CP) forms the capsule that encapsidates the viral genomic ssDNA. We have analyzed the homotypic interaction capacity of full-length and mutated CP. We found that full-length CP interacts with itself. Truncation of the protein from the C-terminal led to diminution of the self-interaction process. Also, the N-terminal region of the CP seemed to be necessary for the interaction. As the two deletion mutants interacted successfully with the wildtype protein, while they failed to self-interact, we suggest that the N-terminal amino acids interact with amino acids of the C-terminal region. Changes in CP homotypic interaction capacity were detected when mutations in the middle portion of the protein were introduced.
authors.affiliation: Department of Genetics, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel.
authors.forename: V
authors.initials: V
authors.lastname: Hallan
authors.forename: Y
authors.initials: Y
authors.lastname: Gafni
mesh_terms: D015153:Blotting, Western; D002213:Capsid / Q000235:genetics / Q000378:metabolism*; D017791:Geminiviridae / Q000235:genetics / Q000502:physiology*; D018551:Solanum lycopersicum / Q000821:virology*; D010935:Plant Diseases / Q000821:virology*; D020798:Two-Hybrid System Techniques; D019065:Virus Assembly