| Literature DB >> 19875079 |
Martin Horn1, Martina Nussbaumerová, Miloslav Sanda, Zuzana Kovárová, Jindrich Srba, Zdenek Franta, Daniel Sojka, Matthew Bogyo, Conor R Caffrey, Petr Kopácek, Michael Mares.
Abstract
Hemoglobin digestion is an essential process for blood-feeding parasites. Using chemical tools, we deconvoluted the intracellular hemoglobinolytic cascade in the tick Ixodes ricinus, a vector of Lyme disease and tick-borne encephalitis. In tick gut tissue, a network of peptidases was demonstrated through imaging with specific activity-based probes and activity profiling with peptidic substrates and inhibitors. This peptidase network is induced upon blood feeding and degrades hemoglobin at acidic pH. Selective inhibitors were applied to dissect the roles of the individual peptidases and to determine the peptidase-specific cleavage map of the hemoglobin molecule. The degradation pathway is initiated by endopeptidases of aspartic and cysteine class (cathepsin D supported by cathepsin L and legumain) and is continued by cysteine amino- and carboxy-dipeptidases (cathepsins C and B). The identified enzymes are potential targets to developing novel anti-tick vaccines.Entities:
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Year: 2009 PMID： 19875079 PMCID： PMC2801564 DOI： 10.1016/j.chembiol.2009.09.009
Source DB: PubMed Journal: Chem Biol ISSN： 1074-5521