Plasmodium falciparum proteinases: cloning of the putative gene coding for the merozoite proteinase for erythrocyte invasion (MPEI) and determination of hydrolysis sites of spectrin by Pf37 proteinase
| Autor: | B. Carcy, Serge Bonnefoy, Isabelle Florent, S L Le Bonniec, Michel Monsigny, Philippe Grellier, D. Dhermy, Roger Mayer, Odile Mercereau-Puijalon, Joseph Schrével |
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| Jazyk: | angličtina |
| Rok vydání: | 1994 |
| Předmět: |
Microbiology (medical)
Erythrocytes lcsh:Arctic medicine. Tropical medicine lcsh:RC955-962 Genes Protozoan Plasmodium falciparum lcsh:QR1-502 erythrocyte invasion lcsh:Microbiology Hydrolysis proteinases Proteinase 3 Putative gene Endopeptidases Animals Spectrin Cloning biology Active site biology.organism_classification In vitro spectrin Biochemistry biology.protein Rabbits |
| Zdroj: | Memórias do Instituto Oswaldo Cruz., Vol 89, Pp 47-49 (1994) Memórias do Instituto Oswaldo Cruz, Volume: 89 Supplement 2, Pages: 47-49, Published: 1994 |
| ISSN: | 1678-8060 0074-0276 |
| Popis: | Numerous proteinase activities have been shown to be essential for the survival of Plasmodium falciparum. One approach to antimalarial chemotherapy, would be to block specifically one or several of these activities, by using compounds structurally analogous to the substrates of these proteinases. Such a strategy requires a detailed knowledge of the active site of the proteinase, in order to identify the best substrate for the proteinase. Aiming at developing such a strategy, two proteinases previously identified in our laboratory, were chosen for further characterization of their molecular structure and properties: the merozoite proteinase for erythrocytic invasion (MPEI), involved in the erythrocyte invasion by the merozoites, and the Pf37 proteinase, which hydrolyses human spectrin in vitro. |
| Databáze: | OpenAIRE |
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