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A distinct member of the aspartic proteinase gene family from the human malaria parasite Plasmodium falciparum
Author(s) -
Berry Colin,
Humphreys Michelle J,
Matharu Philip,
Granger Rachel,
Horrocks Paul,
Moon Richard P,
Certa Uli,
Ridley Robert G,
Bur Daniel,
Kay John
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00276-8
Subject(s) - plasmodium falciparum , biology , parasite hosting , malaria , gene , glycoprotein , gene family , plasmodium (life cycle) , genetics , biochemistry , genome , immunology , world wide web , computer science
A gene ( hap ) transcribed during the intra‐erythrocytic life cycle stages of the human malaria parasite Plasmodium falciparum was cloned and sequenced. It was found to encode a protein belonging to the aspartic proteinase family but which carried replacements of catalytically crucial residues in the hallmark sequences contributing to the active site of this type of proteinase. Consideration is given as to whether this protein is the first known parasite equivalent of the pregnancy‐associated glycoproteins that have been documented in ungulate mammals. Alternatively, it may be operative as a new type of proteinase with a distinct catalytic mechanism. In this event, since no counterpart is known to exist in humans, it affords an attractive potential target against which to develop new anti‐malarial drugs.