1Santé Végétale et Environnement, INRA, BP2078, 06606 Antibes Cedex, France; 2Department of Plant Pathology, Iowa State University, 351 Bessey Hall, Ames 50011, U.S.A.; 3Department of Plant Pathology, University of Georgia, Athens 30602-7274, U.S.A.; 4Nematology, Wageningen Agricultural University, 6709 PD Wageningen, The Netherlands
Go to article:
Accepted 19 March 1999.
A β-1,4-endoglucanase encoding cDNA (EGases, E.C. 188.8.131.52), named Mi-eng-1, was cloned from Meloidogyne incognita second-stage juveniles (J2). The deduced amino acid sequence contains a catalytic domain and a cellulose-binding domain separated by a linker. In M. incognita, the gene is transcribed in the migratory J2, in males, and in the sedentary adult females. In pre-parasitic J2, endoglucanase transcripts are located in the cytoplasm of the subventral esophageal glands. The presence of β-1,4-endoglucanase transcripts in adult females could be related to the expression of the gene in esophageal glands at this stage. However, cellulase activity within the egg matrix of adult females suggests that the endoglucanase may also be synthesized in the rectal glands and involved in the extrusion of the eggs onto the root surface. The maximum identity of the predicted MI-ENG-1 catalytic domain with the recently cloned cyst nematode β-1,4-endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a β-1,4-endoglucanase devoid of a cellulose-binding domain.
The American Phytopathological Society, 1999