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Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity.
Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity.
- Source :
-
Biological chemistry [Biol Chem] 2006 Dec; Vol. 387 (12), pp. 1635-44. - Publication Year :
- 2006
-
Abstract
- Two genes coding for cysteine peptidase inhibitors of the cystatin family (Om-cystatin 1 and 2) were isolated from a gut-specific cDNA library of the soft tick Ornithodoros moubata. Both cystatins were clearly down-regulated after a blood meal. Om-cystatin 1 is mainly expressed in the tick gut, while Om-cystatin 2 mRNA was also found in other tick tissues. Authentic Om-cystatin 2 was significantly more abundant than Om-cystatin 1 in the gut contents of fasting ticks and was associated with hemosome-derived residual bodies accumulated in the gut lumen. Om-cystatin 2 was also expressed by type 2 secretory cells in the salivary glands of unfed ticks. The inhibitory specificity of recombinant Om-cystatins 1 and 2 was tested with mammalian cysteine peptidases, as well as endogenous cysteine peptidases present in the tick gut. Both cystatins efficiently inhibited papain-like peptidases, including cathepsin B and H, but differed significantly in their affinity towards cathepsin C and failed to block asparaginyl endopeptidase. Our results suggest that the secreted cystatin isoinhibitors are involved in the regulation of multiple proteolytic targets in the tick digestive system and tick-host interaction.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
Cystatins chemistry
Cystatins genetics
DNA Primers
DNA, Complementary
Fluorescent Antibody Technique, Indirect
Gene Expression Regulation
Microscopy, Electron
Molecular Sequence Data
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Ticks
Cystatins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1431-6730
- Volume :
- 387
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 17132111
- Full Text :
- https://doi.org/10.1515/BC.2006.204