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

Mitreva, Makedonka and Roze, Erwin and Overmars, Hein and Schots, Ajren and Helder, Johannes and Bakker, Jaap and Smant, Geert (2006) A Symbiont-Independent Endo-1,4-β-Xylanase from the Plant-Parasitic Nematode Meloidogyne incognita. Mol Plant Microbe Interact, 19 (5). pp. 521-529.

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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 inti-
mate 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 polysaccha - rides in plant cell walls independent of endosymbionts. Including our current data on Mi-xyll, we show that the endogenous enzyme complex in root-knot nematode secretions targets essentially all major cell wall carbohydrates to facili-diffusible fragments cleaved from cell wall polysaccharides may act as elicitors of specific disease resistance responses to invading pathogens and parasites (Boudart et al. 1998).

Item Type: Article
Uncontrolled Keywords: cell-wall-degrading enzyme.
Subjects: Medical and Health Sciences > Other medical sciences
Divisions: Faculty of Medical Science
Depositing User: Marija Kalejska
Date Deposited: 30 Nov 2012 10:36
Last Modified: 04 Oct 2013 11:36
URI: https://eprints.ugd.edu.mk/id/eprint/2578

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