Parasite Cathepsin D-Like Peptidases and Their Relevance as Therapeutic Targets
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Review, Research Support, Non-U.S. Gov't
PubMed
27344362
DOI
10.1016/j.pt.2016.05.015
PII: S1471-4922(16)30078-2
Knihovny.cz E-resources
- Keywords
- aspartic peptidases, cathepsin D, hemoglobinolysis, parasites, vectors,
- MeSH
- Antiparasitic Agents pharmacology therapeutic use MeSH
- Enzyme Inhibitors pharmacology MeSH
- Drug Delivery Systems * MeSH
- Parasitic Diseases drug therapy enzymology MeSH
- Parasites enzymology MeSH
- Peptide Hydrolases metabolism MeSH
- Protein Transport genetics MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Antiparasitic Agents MeSH
- Enzyme Inhibitors MeSH
- Peptide Hydrolases MeSH
Inhibition of aspartic cathepsin D-like peptidases (APDs) has been often discussed as an antiparasite intervention strategy. APDs have been considered as virulence factors of Trypanosoma cruzi and Leishmania spp., and have been demonstrated to have important roles in protein trafficking mechanisms of apicomplexan parasites. APDs also initiate blood digestion as components of multienzyme proteolytic complexes in malaria, platyhelminths, nematodes, and ticks. Increasing DNA and RNA sequencing data indicate that parasites express multiple APD isoenzymes of various functions that can now be specifically evaluated using new functional-genomic and biochemical tools, from which we can further assess the potential of APDs as targets for novel effective intervention strategies against parasitic diseases that still pose an alarming threat to mankind.
References provided by Crossref.org
Plasmepsin-like Aspartyl Proteases in Babesia
Protease Inhibition-An Established Strategy to Combat Infectious Diseases
