Abstract:
:Falcipain-2A, the cysteine protease of Plasmodium falciparum has been proposed as a good drug target. This study evaluated the suitability of Plasmodium berghei as the animal model and reports the first functional expression and characterization of the falcipain-2A orthologue, berghepain-2. Comparative studies revealed that the orthologues exhibited different biochemical properties. Berghepain-2 demonstrated optimal activity at a narrower pH optima of 5.5-6 and a lack of preference for substrates with leucine at position 2. Mutagenesis studies revealed roles for residues Val63 and Arg230 of berghepain-2 in contributing to its distinctive biochemical properties. This warrants re-evaluation of employing P. berghei as the murine model for the in vivo screening of falcipain-2A inhibitors. More importantly, these findings stress the underlying importance of establishing the functionality of relevant genes of P. falciparum with concomitant relevance to its murine counterpart prior to its use as the animal model for the screening of potential antimalarials.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Chan C,Goh LL,Sim TSdoi
10.1016/j.femsle.2005.06.024keywords:
subject
Has Abstractpub_date
2005-08-15 00:00:00pages
315-21issue
2eissn
0378-1097issn
1574-6968pii
S0378-1097(05)00400-3journal_volume
249pub_type
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journal_title:FEMS microbiology letters
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pub_type: 杂志文章,评审
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journal_title:FEMS microbiology letters
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journal_title:FEMS microbiology letters
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journal_title:FEMS microbiology letters
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journal_title:FEMS microbiology letters
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pub_type: 杂志文章
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journal_title:FEMS microbiology letters
pub_type: 杂志文章
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