Serological relationships involving potyviral nonstructural proteins.
This report represents a compilation of many of the publications on antigenic properties of potyviral-specified nonstructural proteins. Polyclonal antisera have been prepared for use in characterization of six nonstructural proteins. These include antisera to the cylindrical inclusion proteins of at least 28 potyviruses, to small nuclear inclusion protein (protease) of four potyviruses, to large nuclear inclusion protein (putative replicase) of three viruses, helper component-protease or amorphous inclusion protein of at least four viruses, to the P1 protein (located at the N-terminus of the polyprotein) of one virus, and to the P3 protein (located between helper component protease and cylindrical inclusion protein) of one virus. Monoclonal antibodies also have been prepared to several of these nonstructural proteins. The evidence thus far indicates that cylindrical inclusions of different potyviruses have both conserved and unique epitopes. Nuclear inclusion proteins and amorphous inclusion proteins also may have conserved and unique epitopes. Antigenic relationships of potyviral nonstructural proteins have potential for the identification and classification of potyviruses.
Purcifull
D E
DE
Department of Plant Pathology, University of Florida, Gainesville.
Hiebert
E
E
D010942:Plant Viruses / Q000145:classification / Q000276:immunology*; D012328:RNA Viruses / Q000145:classification / Q000276:immunology*; D012703:Serotyping; D017361:Viral Nonstructural Proteins / Q000276:immunology*
D017361:Viral Nonstructural Proteins