cDNA cloning of a novel cysteine protease of Plasmodium falciparum

被引:9
作者
Hanspal, M [1 ]
机构
[1] Tufts Univ, Sch Med, St Elizabeths Med Ctr, Div Hematol Res, Boston, MA 02135 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 2000年 / 1493卷 / 1-2期
关键词
malaria; cysteine protease; erythrocyte; Plasmodium falciparum;
D O I
10.1016/S0167-4781(00)00159-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The cDNA for a novel Plasmodium cysteine protease (falcipain-2) has been isolated from a Plasmodium falciparum cDNA library. A 602 bp fragment was amplified from P. falciparum by PCR using degenerate oligonucleotide primers. The primers were designed based upon the amino acids flanking the active site cysteine and asparagine residues that are conserved in the eukaryotic cysteine proteases. This fragment was used to screen a P. falciparum cDNA library and isolated a 2.1 kb clone that encoded a novel cysteine protease. The sequence of the 2.1 kb clone predicted a 56 kDa protein containing a typical signal sequence, a prosequence and a 24.7 kDa mature protease with 37% identity to falcipain-1, a hemoglobin-degrading cysteine protease of P. falciparum. Northern blot analysis detected a 2.1 kb message in trophozoites. Taken together, we have isolated a novel cysteine protease of P. falciparum, which may play an important role at the late stages of the erythrocytic cycle of the parasite. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:242 / 245
页数:4
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