Characterization of a cDNA encoding a cathepsin L-like protein of Rhodnius prolixus

• Published in: Insect molecular biology 2001-10, Vol.10 (5), p.505-511
• Main Authors: Lopez-Ordoñez, T., Rodriguez, M. H., de la Cruz Hernández-Hernández, F.
• Format: Article
• Language: English
• Subjects: 3' Untranslated Regions - genetics; 5' Untranslated Regions - genetics; Amino Acid Sequence; Animals; Arthropods - genetics; Base Sequence; Cathepsin L; Cathepsins - genetics; Cysteine Endopeptidases; cysteine protease; Digestive System - enzymology; DNA, Complementary - genetics; intestine; Molecular Sequence Data; Phylogeny; Protein Precursors - genetics; Reduviidae; Rhodnius - classification; Rhodnius - enzymology; Rhodnius - genetics; Rhodnius prolixus; RpCat gene; secretion; Sequence Alignment; Sequence Homology, Amino Acid; Trypanosoma brucei; Trypanosoma cruzi - parasitology
• ISSN: 0962-1075; 1365-2583
• DOI: 10.1046/j.0962-1075.2001.00290.x

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.