Application of a putative fatty-acid binding protein to discriminate serologically the two European quarantine root-knot nematodes, Meloidogyne chitwoodi and M. fallax, from other Meloidogyne species |
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Authors: | Christophe Tastet, Florence Val, Michel Lesage, Lionel Renault, Laurent Marché , Michel Bossis Didier Mugnié ry |
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Affiliation: | (1) INRA/ENSAR – UMR BiO3P, Domaine de la Motte, B.P. 35357, 35653 Le Rheu Cedex, France;(2) INRA/ENSAR – UMR BiO3P, Domaine de la Motte, B.P. 35357, 35653 Le Rheu Cedex, France |
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Abstract: | Two major proteins, Mcf-A67 and Mcf-B66, were identified by mini two-dimensional polyacrylamide gel electrophoresis in order to distinguish the two European quarantine root-knot nematodes, Meloidogyne chitwoodi and M. fallax, from eight other species. These quarantine proteinic markers have been microsequenced after enzymatic digestion. The internal amino acid sequences exhibit similarities to members of a family of low molecular weight intracellular lipid-binding proteins. Moreover, to explore a simple, rapid, and inexpensive way to identify the two quarantine nematodes, dot blot hybridizations were performed using an antiserum ( A67) produced from the longest amino-acid sequence of the protein Mcf-A67. Although several proteins stained on the M. chitwoodi and M. fallax western blot membranes, the two nematodes were easily distinguished from other root-knot nematodes, on dot blot assays with soluble proteins extracted from a single female. Because of its specificity and sensitivity, the use of the A67 antiserum to improve the diagnosis of the two European quarantine root-knot nematodes is discussed. |
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Keywords: | FABP internal amino acid sequencing polyclonal antibodies root-knot nematode two-dimensional polyacrylamide gel electrophoresis |
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