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Pierre Abad - One of the best experts on this subject based on the ideXlab platform.
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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-par...
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A beta-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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 beta-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 beta-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a beta-1,4-Endoglucanase devoid of a cellulose-binding domain.
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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
Marie-noëlle Rosso - One of the best experts on this subject based on the ideXlab platform.
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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-par...
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A beta-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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 beta-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 beta-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a beta-1,4-Endoglucanase devoid of a cellulose-binding domain.
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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
Evelyne Forano - One of the best experts on this subject based on the ideXlab platform.
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Endoglucanase activity and relative expression of glycoside hydrolase genes of Fibrobacter succinogenes S85 grown on different substrates.
Biochimica et biophysica acta, 2000Co-Authors: Christel Béra Maillet, Geneviève Gaudet, Evelyne ForanoAbstract:Abstract The Endoglucanase activity of cells and extracellular culture fluid of Fibrobacter succinogenes S85 grown on glucose, cellobiose, soluble polysaccharides (β-glucan, lichenan) and intact plant polysaccharides, was compared. The specific activity of cells grown on cellulose or forages was 6- to 20-fold higher than that of cells grown on soluble substrates, suggesting an induction of Endoglucanases by the insoluble substrates. The ratios of cells to extracellular culture fluid Endoglucanase activities measured in cultures grown on sugars or insoluble polysaccharides suggested that the Endoglucanases induced by the insoluble polysaccharides remained attached to the cells. The mRNA of all the F. succinogenes glycoside hydrolase genes sequenced so far were then quantified in cells grown on glucose, cellobiose or cellulose. The results show that all these genes were transcribed in growing cells, and that they are all overexpressed in cultures grown on cellulose. Endoglucanase-encoding endB and endAFS genes, and xylanase-encoding xynC gene appeared the most expressed genes in growing cells. EGB and ENDA are thus likely to play a major role in cellulose degradation in F. succinogenes.
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Endoglucanase activity and relative expression of glycoside hydrolase genes of Fibrobacter succinogenes S85 grown on different substrates
BBA - Biochimica et Biophysica Acta, 2000Co-Authors: Christel Béra Maillet, Gérard Gaudet, Evelyne ForanoAbstract:The Endoglucanase activity of cells and extracellular culture fluid of Fibrobacter succinogenes S85 grown on glucose, cellobiose, soluble polysaccharides (beta -glucan, lichenan) and intact plant polysaccharides, was compared. The specific activity of cells grown on cellulose or forages was 6- to 20-fold higher than that of cells grown on soluble substrates, suggesting an induction of Endoglucanases by the insoluble substrates. The ratios of cells to extracellular culture fluid Endoglucanase activities measured in cultures grown on sugars or insoluble polysaccharides suggested that the Endoglucanases induced by the insoluble polysaccharides remained attached to the cells. The mRNA of all the F. succinogenes glycoside hydrolase genes sequenced so far were then quantified in cells grown on glucose, cellobiose or cellulose. The results show that all these genes were transcribed in growing cells, and that they are all overexpressed in cultures grown on cellulose. Endoglucanase-encoding endB and endA(FS) genes, and xylanase-encoding xynC gene appeared the most expressed genes in growing cells. EGB and ENDA are thus likely to play a major role in cellulose degradation in F. succinogenes.
Bruno Favery - One of the best experts on this subject based on the ideXlab platform.
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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-par...
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A beta-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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 beta-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 beta-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a beta-1,4-Endoglucanase devoid of a cellulose-binding domain.
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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
Jan M. De Boer - One of the best experts on this subject based on the ideXlab platform.
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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-par...
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isolation of a cdna encoding a β 1 4 Endoglucanase in the root knot nematode meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A beta-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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 beta-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 beta-1,4-Endoglucanases is 52.5%. In contrast to cyst nematodes, M. incognita pre-parasitic J2 were not found to express a beta-1,4-Endoglucanase devoid of a cellulose-binding domain.
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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
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Isolation of a cDNA encoding a β-1,4-Endoglucanase in the root-knot nematode Meloidogyne incognita and expression analysis during plant parasitism
Molecular Plant-Microbe Interactions, 1999Co-Authors: Marie-noëlle Rosso, Jaap Bakker, Richard S Hussey, Thomas J Baum, Bruno Favery, Christine Piotte, Laury Arthaud, Jan M. De Boer, Pierre AbadAbstract:A β-1,4-Endoglucanase encoding cDNA (EGases, E.C. 3.2.1.4), 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