Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 275, Issue 14, Pages 10331-10341Publisher
ELSEVIER
DOI: 10.1074/jbc.275.14.10331
Keywords
-
Categories
Ask authors/readers for more resources
The Plasmodium ookinete produces chitinolytic activity that allows the parasite to penetrate the chitin-containing peritrophic matrix surrounding the blood meal in the mosquito midgut, Since the peritrophic matrix is a physical barrier that the parasite must cross to invade the mosquito, and the presence of allosamidin, a chitinase inhibitor, in a blood meal prevents the parasite from invading the midgut epithelium, chitinases (3.2.1.14) are potential targets of malaria parasite transmission-blocking interventions. We have purified a chitinase of the avian malaria parasite Plasmodium gallinaceum and cloned the gene, PgCHT1, encoding it. PgCHT1 encodes catalytic and substrate-binding sites characteristic of family 18 glycohydrolases, Expressed in Escherichia coli strain AD494 (DE3), recombinant PgCHT1 was found to hydrolyze polymeric chitin, native chitin oligosaccharides, and 4-methylumbelliferone derivatives of chitin oligosaccharides. Allosamidin inhibited recombinant PgCHT1 with an IC50 of 7 mu M and differentially inhibited two chromatographically separable P. gallinaceum ookinete-produced chitinase activities with IC50 values of 7 and 12 mu M, respectively, These two chitinase activities also had different pH activity profiles. These data suggest that the P, gallinaceum oo kinete uses products of more than one chitinase gene to initiate mosquito midgut invasion.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available