Biochemical characterization of MI-ENG1, a family 5 endoglucanase secreted by the root-knot nematode Meloidogyne incognita.
A beta-1,4-endoglucanase named MI-ENG1, homologous to the family 5 glycoside hydrolases, was previously isolated from the plant parasitic root-knot nematode Meloidogyne incognita. We describe here the detection of the enzyme in the nematode homogenate and secretion and its complete biochemical characterization. This study is the first comparison of the enzymatic properties of an animal glycoside hydrolase with plant and microbial enzymes. MI-ENG1 shares many enzymatic properties with known endoglucanases from plants, free-living or rumen-associated microorganisms and phytopathogens. In spite of the presence of a cellulose-binding domain at the C-terminus, the ability of MI-ENG1 to bind cellulose could not be demonstrated, whatever the experimental conditions used. The biochemical characterization of the enzyme is a first step towards the understanding of the molecular events taking place during the plant-nematode interaction.
Béra-Maillet
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INRA, Unité Santé Végétale et Environnement, Antibes, France.
Arthaud
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Abad
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Rosso
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MN
D000595:Amino Acid Sequence; D000818:Animals; D002266:Carboxymethylcellulose Sodium / Q000378:metabolism; D002413:Cations, Divalent; D002480:Cellulase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology; D002482:Cellulose / Q000378:metabolism; D002614:Chelating Agents / Q000494:pharmacology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004492:Edetic Acid / Q000494:pharmacology; D004926:Escherichia coli; D005936:Glucans / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000145:classification / Q000378:metabolism; D015801:Helminth Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology; D006790:Host-Parasite Interactions; D008969:Molecular Sequence Data; D018517:Plant Roots / Q000469:parasitology; D010947:Plants, Toxic; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014026:Nicotiana / Q000166:cytology; D014431:Tylenchoidea / Q000201:enzymology* / Q000502:physiology; D014990:Xylans / Q000378:metabolism
D002413:Cations, Divalent; D002614:Chelating Agents; D005936:Glucans; D015801:Helminth Proteins; D011993:Recombinant Fusion Proteins; D014990:Xylans; D002482:Cellulose; D004492:Edetic Acid; D006026:Glycoside Hydrolases; C097231:endoglucanase V; D002480:Cellulase; D002266:Carboxymethylcellulose Sodium