Serological differentiation of the potato-cyst nematodesGlobodera pallidaand G.rostochiensis: partial purification of species-specific proteins

Abstract

SUMMARYTwo major groups of heat-stable proteins have been purified by heat denaturation from homogenates of eggs of the potato-cyst nematodesGlobodera rostochiensisandG. pallida.SDS-polyacrylamide gel electrophoresis of protein homogenates from 6G. rostochiensispopulations and 7G. pallidapopulations revealed 2 bands specific forG. rostochiensisand 3 bands specific forG. pallida.Two-dimensional electrophoresis showed that the 2 bands specific forG. rostochiensisconsisted of 2 polypeptides differing slightly in isoelectric point, as did one of the bands specific forG. pallida.Conventional antisera made against protein homogenates of eitherGloboderaspecies showed a complete cross-reaction with the species-specific proteins. The perspectives of the differences in protein composition betweenG. rostochiensisandG. pallida, established in this study, for a quantitative differentiation of mixed field populations of the twoGloboderaspecies, involving monoclonal antibodies, are discussed.