Activity and sequence characterization of two cysteine proteases in the digestive tract of the reduviid bug Triatoma infestans

Cathepsin B- and cathepsin L-like activities were identified in gut extracts of the blood-sucking bug Triatoma infestans using specific substrates and inhibitors. Activities decreased during the first 2 days after feeding but increased to a maximum value at 5 and 10 days post feeding. The deduced 33...

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Bibliographic Details
Published in:Insect molecular biology 2004-12, Vol.13 (6), p.569-579
Main Authors: Kollien, A.H, Waniek, P.J, Nisbet, A.J, Billingsley, P.F, Schaub, G.A
Format: Article
Language:English
Subjects:
active sites
Amino Acid Sequence
amino acid sequences
Animals
Base Sequence
cathepsin B
Cathepsin B - genetics
Cathepsin B - metabolism
Cathepsin L
cathepsins
Cathepsins - genetics
Cathepsins - metabolism
cathepsin B
cathepsin L
complementary DNA
Cysteine Endopeptidases - genetics
Cysteine Endopeptidases - metabolism
cysteine proteinase
cysteine proteinases
digestive enzymes
DNA Primers
Eating - physiology
enzyme activity
enzyme inhibitors
enzyme substrates
Gastrointestinal Tract - metabolism
gene expression
Gene Expression Profiling
hematophagy
midgut
Molecular Sequence Data
Nucleic Acid Amplification Techniques
nucleotide sequences
Reduviidae
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Analysis, DNA
Triatoma - enzymology
Triatoma - physiology
Triatoma infestans
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Summary:Cathepsin B- and cathepsin L-like activities were identified in gut extracts of the blood-sucking bug Triatoma infestans using specific substrates and inhibitors. Activities decreased during the first 2 days after feeding but increased to a maximum value at 5 and 10 days post feeding. The deduced 332 and 328 amino acid sequences showed high levels of identity (50-60%) to other insect cathepsin B- and L-like proteases, respectively. The three amino acid residues of the catalytic domain, CHN, and the GCNGG motif were conserved in both cathepsins, but the occluding loop, characterizing B-like cathepsins, was present only in one. ERFNIN and GNFD motifs occurred in the other sequence, defining it as cathepsin L-like. The cathepsin B-like gene was expressed at low, constitutive levels in unfed and fed T. infestans.
ISSN:0962-1075
1365-2583
DOI:10.1111/j.0962-1075.2004.00504.x