TY - JOUR
T1 - Plasmodium falciparum GPI mannosyltransferase-III has novel signature sequence and is functional
AU - Basagoudanavar, Suresh H.
AU - Feng, Xiaorong
AU - Krishnegowda, Gowdahalli
AU - Muthusamy, Arivalagan
AU - Gowda, D. Channe
N1 - Funding Information:
This work was supported by grant AI 41139 from NIAID, National Institutes of Health.
PY - 2007/12/28
Y1 - 2007/12/28
N2 - The glycosylphosphatidylinositol (GPI) anchors of Plasmodium falciparum are indispensable for parasite survival since merozoite surface proteins-1, -2, -4, -5, and -10, crucial for erythrocyte invasion, are GPI-anchored. Therefore, the GPI biosynthetic pathway can offer potential targets for novel anti-malarial drugs. Here, we characterized the putative P. falciparum PIG-B gene (PfPIGB) that encodes mannosyltransferase-III of GPI biosynthesis. PfPIGB mRNA is transcribed in a developmental stage specific manner. A protein corresponding to the expected size of PfPIG-B is expressed by the parasite and is localized in the endoplasmic reticulum. Treatment of parasites with PfPIG-B specific siRNA caused reduction in GPI synthesis, affecting the PIG-B specific GPI intermediate. These data demonstrate that PfPIG-B is functional and encodes mannosyltransferase-III of the parasite GPI biosynthesis. The parasite PfPIG-B is novel in that its signature sequence HKEHKI is unique and is only partially conserved as compared to HKEXRF signature motif of mammalian PIG-B enzymes.
AB - The glycosylphosphatidylinositol (GPI) anchors of Plasmodium falciparum are indispensable for parasite survival since merozoite surface proteins-1, -2, -4, -5, and -10, crucial for erythrocyte invasion, are GPI-anchored. Therefore, the GPI biosynthetic pathway can offer potential targets for novel anti-malarial drugs. Here, we characterized the putative P. falciparum PIG-B gene (PfPIGB) that encodes mannosyltransferase-III of GPI biosynthesis. PfPIGB mRNA is transcribed in a developmental stage specific manner. A protein corresponding to the expected size of PfPIG-B is expressed by the parasite and is localized in the endoplasmic reticulum. Treatment of parasites with PfPIG-B specific siRNA caused reduction in GPI synthesis, affecting the PIG-B specific GPI intermediate. These data demonstrate that PfPIG-B is functional and encodes mannosyltransferase-III of the parasite GPI biosynthesis. The parasite PfPIG-B is novel in that its signature sequence HKEHKI is unique and is only partially conserved as compared to HKEXRF signature motif of mammalian PIG-B enzymes.
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U2 - 10.1016/j.bbrc.2007.10.061
DO - 10.1016/j.bbrc.2007.10.061
M3 - Article
C2 - 17977514
AN - SCOPUS:36048986477
SN - 0006-291X
VL - 364
SP - 748
EP - 754
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -