Features on the surface of the tobacco rattle tobravirus particle that are antigenic and sensitive to proteolytic digestion.
The particle proteins of tobraviruses and tobamoviruses share six sequence motifs, two of which are also present in furoviruses and hordeiviruses. Analyses of four different polyclonal antisera to tobacco rattle tobravirus by Pepscan revealed that the C-terminal region of the particle protein was immunodominant. The N-terminal region and a central region (residues 110-121) were more weakly immunogenic. These results suggest that these regions are exposed externally on the assembled virus particle. Papain digestion showed that the C terminus can be removed without apparent structural damage to the particle. The external location of the C-terminal region along the sides of the particle could explain some transmission properties of the rod-shaped viruses.
Legorburu
F J
FJ
Scottish Crop Research Institute, Invergowrie, Dundee, UK.
Robinson
D J
DJ
Torrance
L
L
D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D010206:Papain / Q000494:pharmacology; D010942:Plant Viruses / Q000737:chemistry*; D011817:Rabbits; D014764:Viral Proteins / Q000737:chemistry* / Q000276:immunology
D014764:Viral Proteins; D010206:Papain