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Updated: Jun 28, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Meloidogyne incognita: molecular cloning and characterization of a cDNA encoding a cathepsin D-like aspartic
Rodrigo da Rocha Fragoso1, Isabela Tristan Lourenço, João Aguiar Nogueira Batista
1Embrapa, Cerrados, Planaltina, DF, Brazil.
Abstract:
Herein we describe the cloning and characterization of a cDNA encoding an aspartic proteinase from the root-knot nematode Meloidogyne incognita. Using PCR techniques, a 1471-bp cDNA fragment encoding a cathepsin D-like (Mi-asp1) transcript was isolated from second-stage larvae mRNA. Its predicted amino acid sequence comprises a pro-region of 71 amino acid residues and a mature protease of 378 amino acid residues with a predicted molecular mass of 41.502kDa. Protein sequence comparisons of Mi-asp1 with GenBank (DQ360827) sequences showed 59-71% identity with nematode-specific cathepsin D-like aspartic proteinases. Southern blot analysis, RT-PCR amplification and EST mining suggest the existence of a developmentally expressed gene family encoding aspartic proteinases in M. incognita. Mi-asp1 may represent a potential target for molecular intervention for the purposes of plant-parasitic nematode control.

