TABLE CONTENTS

SESSION FIFTEEN – FOREST NEMATOLOGY AND PINE WILT
DISEASE
CONVENORS: KAZUYOSHI FUTAI & CHRISTER MAGNUSSON
Bursaphelenchus xylophilus Surface Proteins: Stage-specific Changes and
Characterization
Shinya, R., Y. Takeuchi, N. Miura, M. Ueda. & K. Futai
Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
The surface coat (SC) proteins of plant-parasitic nematodes are likely to play a key role in
plant-nematode interactions. It has been demonstrated that an important feature of the SC
protein is its lability. In the present study, several kinds of lectins were tested for their
binding characteristics to the SC proteins of the pine wood nematode, Bursaphelenchus
xylophilus, to detect the stage- and isolate-specific changes of SC proteins. Furthermore, the
characterizations of SC proteins were conducted by using some molecular techniques. The
results demonstrated the stage-specific differences in binding characteristics of a lectin, wheat
germ agglutinin (WGA). WGA binding was observed only to the outer surfaces of third-stage
propagative juveniles and to the egg shells. Such bindings were detected at higher frequency
in virulent isolates than in avirulent isolates. A greater variety of lectins bound to eggs than to
other stages. In contrast, no lectin bound to the outer cuticles of dispersal stage juveniles. For
characterization, the SC proteins were extracted and separated by sodium dodecyl sulfatepolyacrylamide
gel electrophoresis (SDS-PAGE). SDS-PAGE analysis detected various SC
proteins and some of them differed among the stages of B. xylophilus. Since the most SC
proteins were proved to be glycosylated, these glycosylations were investigated in detail by
lectin blot analysis. In this presentation, we will also present other characteristics of the SC
proteins of the nematode and discuss a possible role of these developmental changes in SC
proteins in pine-B. xylophilus interactions.
5 th International Congress of Nematology, 2008 55