Background: Triatoma infestans (Hemiptera: Reduviidae) is a hematophagous insect and the main vector of Trypanosoma cruzi (Kinetoplastida: Trypanosomatidae). In the present study, the authors investigated whether a serine protease activity from the saliva of T. infestans has a role in vasomotor modulation, and in the insect-blood feeding by cleaving and activating protease-activated receptors (PARs). Methods: T. infestans saliva was chromatographed as previously reported for purification of triapsin, a serine protease. The cleavage activity of triapsin on PAR peptides was investigated based on FRET technology. Mass spectrometry was used to analyze the sites of PAR-2 peptide cleaved by triapsin. NO measurements were performed using the DAN assay (2,3-diaminonapthalene). The vasorelaxant activity of triapsin was measured in vessels with or without functional endothelium pre-contracted with phenylephrine (3 µM). Intravital microscopy was used to assess the effect of triapsin on mouse skin microcirculation. Results: Triapsin was able to induce hydrolysis of PAR peptides and showed a higher preference for cleavage of the PAR-2 peptide. Analysis by mass spectrometry confirmed a single cleavage site, which corresponds to the activation site of the PAR-2 receptor.
CITATION STYLE
Oliveira, K. A., Torquato, R. J. S., Garcia Lustosa, D. C. G., Ribeiro, T., Nascimento, B. W. L., de Oliveira, L. C. G., … Tanaka, A. S. (2021). Proteolytic activity of Triatoma infestans saliva associated with PAR-2 activation and vasodilation. Journal of Venomous Animals and Toxins Including Tropical Diseases, 27. https://doi.org/10.1590/1678-9199-JVATITD-2020-0098
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