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Serological differentiation of the potato-cyst nematodes Globodera pallida and G. rostochiensis: partial purification of species-specific proteins

Published online by Cambridge University Press:  06 April 2009

A. Schots
Affiliation:
Department of Nematology, Agricultural University, Binnenhaven 10, 6709 PD Wageningen, The Netherlands Department of Experimental Animal Morphology and Cell Biology, Agricultural University, Marijkeweg 40, 6709 PG Wageningen, The Netherlands
J. Bakker
Affiliation:
Department of Nematology, Agricultural University, Binnenhaven 10, 6709 PD Wageningen, The Netherlands
F. J. Gommers
Affiliation:
Department of Nematology, Agricultural University, Binnenhaven 10, 6709 PD Wageningen, The Netherlands
L. Bouwman-Smits
Affiliation:
Department of Nematology, Agricultural University, Binnenhaven 10, 6709 PD Wageningen, The Netherlands
E. Egberts
Affiliation:
Department of Experimental Animal Morphology and Cell Biology, Agricultural University, Marijkeweg 40, 6709 PG Wageningen, The Netherlands

Summary

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

Type
Research Article
Copyright
Copyright © Cambridge University Press 1987

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