Journal
PHYSIOLOGICAL AND MOLECULAR PLANT PATHOLOGY
Volume 63, Issue 3, Pages 159-165Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pmpp.2003.10.005
Keywords
cathepsin L protease; developmental expression; intestinal cells; Meloidogyne incognita; plant-parasitic nematode; virulence
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A cathepsin L protease full-length cDNA (named Mi-cpl-1) was characterised front infective second-stage juveniles of the root-knot nematode Meloidogyne incognita by SL1-primed PCR and 3' rapid amplification of cDNA ends (3'-RACE). A single open reading frame was identified. encoding a putative 383-amino acid protein predicted to contain a putative N-terminal short secretion signal peptide, which suggests that Mi-CPL-1 Should function as an extracellular protein. The putative mature enzyme included several conserved amino acid residues/motives, among which the typical catalytic triad of the active site. In situ mRNA hybridization analyses showed that transcripts of Mi-cpl-1 accumulated specifically in the intestinal cells of specimens. which suggests that the protein could be involved in the digestive processes of the nematode. However, expression of Mi-cpl-1 was shown to occur exclusively in the developmental stages which are in close interaction with the root tissues (i.e. second-stage juveniles and females). This may indicate that some function of the cathepsin L cysteine protease in M. incognita is more directly related to the parasitic aspects of the plant-nematode relationship, e.g. pathogenicity and/or evasion of primary host plant defence systems. (C) 2003 Elsevier Ltd. All rights reserved.
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