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Endogenous cellulases in animals: isolation of b-1,4-endoglucanase genes from two species of plant-parasitic cyst nematodes

, : Endogenous cellulases in animals: isolation of b-1,4-endoglucanase genes from two species of plant-parasitic cyst nematodes. Proceedings of the National Academy of Sciences of the United States of America 95(9): 06-11

Four b-1,4-endoglucanases (EGases) from the cyst nematodes Globodera rostochiensis and Heterodera glycines were characterized. The 4 catalytic domains belonged to family 5 of the glycosyl hydrolases and showed 37-44 percent amino acid identity with EGases from the bacteria Erwinia chrysanthemi, Clostridium acetobutylicum, and Bacillus subtilis. Each of the nematode species possessed an EGase with a bacterial-type cellulose-binding domain, but the EGases were not of bacterial origin. It is presumed that the nematode EGases aid intracellular migration through plant roots via partial cell wall degradation. Sequence data were deposited in the sequence data banks under the accession nos. AF006052-3, AF004523, and AF004716.


DOI: 10.2307/44639

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