Publicação
The activity and inhibition of the food vacuole plasmepsin from the rodent malaria parasite Plasmodium chabaudi
| Resumo: | The rodent malaria parasite Plasmodium chabaudi encodes one food vacuole plasmepsin - the aspartic proteinases important in haemoglobin degradation. A recombinant form of this enzyme was found to cleave a variety of peptide substrates and was susceptible to a selection of naturally occurring and synthetic inhibitors, displaying an inhibition profile distinct from that of aspartic proteinases from other malaria parasites. In addition, inhibitors of HIV proteinase that kill P. chabaudi in vivo were also inhibitors of this new plasmepsin. P. chabaudi is a widely used model for human malaria species and, therefore, the characterisation of this plasmepsin is an important contribution towards understanding its biology. |
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| Autores principais: | Martins, Tiago M. |
| Outros Autores: | Domingos, Ana; Berry, Colin; Wyatt, David M. |
| Assunto: | Aspartic proteinase New plasmepsin Plasmodium chabaudi Rodent malaria model Parasitology veterinary (miscalleneous) Insect Science Infectious Diseases SDG 3 - Good Health and Well-being |
| Ano: | 2006 |
| País: | Portugal |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Universidade Nova de Lisboa |
| Idioma: | inglês |
| Origem: | Repositório Institucional da UNL |
| Resumo: | The rodent malaria parasite Plasmodium chabaudi encodes one food vacuole plasmepsin - the aspartic proteinases important in haemoglobin degradation. A recombinant form of this enzyme was found to cleave a variety of peptide substrates and was susceptible to a selection of naturally occurring and synthetic inhibitors, displaying an inhibition profile distinct from that of aspartic proteinases from other malaria parasites. In addition, inhibitors of HIV proteinase that kill P. chabaudi in vivo were also inhibitors of this new plasmepsin. P. chabaudi is a widely used model for human malaria species and, therefore, the characterisation of this plasmepsin is an important contribution towards understanding its biology. |
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