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A novel cell wall
degrading enzyme in the plant parasitic nematode Meloidogyne incognita. M. DAUTOVA (1), H. Overmars
(1), A. Schots (2), F. J. Gommers (1), J. Bakker (1), and G. Smant (1). (1)
Laboratories of Nematology; (2) Monoclonal Antibodies, WUR, Binnenhaven 10,
6709 PD Wageningen, The Netherlands. Phytopathology 91:S21. Publication no.
P-2001-0146-AMA. Single pass 5-prime end sequencing of approximately 1,000 clones from a cDNA library constructed of preparasitic M. incognita J2 has revealed a partial sequence with a homology to xylanases of various bacterial origin. This expressed sequence tag was used to obtain a full-length transcript of 1220 nt encoding an open reading frame (Mi-xyl1) of 34,9 kDa. Hydrophobic cluster analysis classified the putative xylanase as a type 5 glycosyl hydrolase. Whole mount in situ hybridization showed specific labeling of the Mi-xyl1 in the subventral esophageal glands of second stage juveniles. DNA blot hybridization indicated the presence of two homologues in M. incognita whereas no hybridization was found on genomic DNA fragments of C. elegans and cyst nematodes. Recombinant Mi-xyl1 protein exhibited hydrolytic activity on xylan and carboxymethyl cellulose. Conclusively, root knot nematodes (Meloidogyne spp.) make use of a suite of cell wall degrading enzymes with overlapping activities to facilitate plant invasion. |
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