有哪些信誉好的足球投注网站an egf-like protein forms a complex with pfrh5 and is required for invasion of human erythrocytes by plasmodium falciparum一种egf-like蛋白质与pfrh5形式复杂,所需由恶性疟原虫入侵人类红细胞.pdfVIP
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an egf-like protein forms a complex with pfrh5 and is required for invasion of human erythrocytes by plasmodium falciparum一种egf-like蛋白质与pfrh5形式复杂,所需由恶性疟原虫入侵人类红细胞
An EGF-like Protein Forms a Complex with PfRh5 and Is
Required for Invasion of Human Erythrocytes by
Plasmodium falciparum
1,2 1 1,2 3 1 1,2
Lin Chen , Sash Lopaticki , David T. Riglar , Chaitali Dekiwadia , Alex D. Uboldi , Wai-Hong Tham ,
1 1 1,2 3 1,2
Matthew T. O’Neill , Dave Richard , Jake Baum , Stuart A. Ralph , Alan F. Cowman *
1The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia, 2 Department of Medical Biology, University of Melbourne, Melbourne, Australia,
3 Department of Biochemistry and Molecular Biology, Bio21 Molecular Sciences and Biotechnology Institute, University of Melbourne, Melbourne, Australia
Abstract
Invasion of erythrocytes by Plasmodium falciparum involves a complex cascade of protein-protein interactions between
parasite ligands and host receptors. The reticulocyte binding-like homologue (PfRh) protein family is involved in binding to
and initiating entry of the invasive merozoite into erythrocytes. An important member of this family is PfRh5. Using ion-
exchange chromatography, immunoprecipitation and mass spectroscopy, we have identified a novel cysteine-rich protein
we have called P. falciparum Rh5 interacting protein (PfRipr) (PFC1045c), which forms a complex with PfRh5 in merozoites.
Mature PfRipr has a molecular weight of 123 kDa with 10 epidermal growth factor-like domains and 87 cysteine residues
distributed along the protein. In mature schizont stages this protein is processed into two polypeptides that associate and
form a complex with
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