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A Symbiont-Independent Endo-1,4-β-Xylanase from the Plant-Parasitic Nematode Meloidogyne incognita

May 2006 , Volume 19 , Number  5
Pages  521 - 529

Makedonka Mitreva-Dautova , 1 Erwin Roze , 2 Hein Overmars , 2 Leo de Graaff , 3 Arjen Schots , 4 Johannes Helder , 2 Aska Goverse , 2 Jaap Bakker , 2 and Geert Smant 2

1Genome Sequencing Centre, Department of Genetics, Washington University School of Medicine, St. Louis, MO 63108, U.S.A.; 2Laboratory of Nematology, 3Laboratory of Microbiology, and 4Laboratory of Molecular Recognition and Antibody Technology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, The Netherlands

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Accepted 20 January 2006.

Substituted xylan polymers constitute a major part of the hemicellulose fraction of plant cell walls, especially in monocotyledons. Endo-1,4-β-xylanases (EC are capable of hydrolyzing substituted xylan polymers into fragments of random size. Many herbivorous animals have evolved intimate relationships with endosymbionts to exploit their enzyme complexes for the degradation of xylan. Here, we report the first finding of a functional endo-1,4-β-xylanase gene from an animal. The gene (Mi-xyl1) was found in the obligate plant-parasitic root-knot nematode Meloidogyne incognita, and encodes a protein that is classified as a member of glycosyl hydrolase family 5. The expression of Mi-xyl1 is localized in the subventral esophageal gland cells of the nematode. Previous studies have shown that M. incognita has the ability to degrade cellulose and pectic polysaccharides in plant cell walls independent of endosymbionts. Including our current data on Mi-xyl1, we show that the endogenous enzyme complex in root-knot nematode secretions targets essentially all major cell wall carbohydrates to facilitate a stealthy intercellular migration in the host plant.

Additional keywords: cell-wall-degrading enzyme.

© 2006 The American Phytopathological Society