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Characterization of a cDNA encoding a cathepsin L‐like protein of Rhodnius prolixus
Author(s) -
LopezOrdoñez T.,
Rodriguez M. H.,
de la Cruz HernándezHernández F.
Publication year - 2001
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.0962-1075.2001.00290.x
Subject(s) - rhodnius prolixus , biology , complementary dna , signal peptide , peptide sequence , microbiology and biotechnology , cathepsin , cathepsin b , messenger rna , biochemistry , cathepsin h , gene , enzyme , ecology , insect
The interaction of Rhodnius prolixus digestive enzymes with Trypanosoma cruzi could be important for parasite survival. We report herein the complete sequence of the messenger of a cathepsin L‐like molecule (RpCat). The cDNA has 5′‐ and 3′‐ end UTRs and a methionine codon that corresponds likely to a translation initiation codon. In the deduced amino acid sequence, a region corresponding to an ERFININ domain, diagnostic of L‐cathepsins, and a possible pro‐peptide cleavage site were observed. At the C‐terminus, a nine‐amino acid sequence, almost identical to a secretion signal of human cathepsin L was found. RpCat messenger was expressed in intestines of R. prolixus adults, and from 1st to 4th but not in 5th instar nymph stages. In a similarity analysis, RpCat was grouped with L cathepsins forming a clear group separate of the B cathepsins.