Studies of the molecules form plasmodium falciparum that mediate pathogenesis

Adhesion of erythrocytes infected by Plasmodium falciparum to receptors of the microvasculature is a major contributor of parasite pathology and morbidity. It is mediated by the P. falciparum erythrocyte membrane protein 1 (PfEMP-1) which is expressed at the surface of infected erythocytes and is li...

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Main Author: Mo, Min
Other Authors: Julien Lescar
Format: Theses and Dissertations
Published: 2008
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Online Access:https://hdl.handle.net/10356/6566
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-65662023-02-28T18:39:52Z Studies of the molecules form plasmodium falciparum that mediate pathogenesis Mo, Min Julien Lescar School of Biological Sciences DRNTU::Science::Biological sciences Adhesion of erythrocytes infected by Plasmodium falciparum to receptors of the microvasculature is a major contributor of parasite pathology and morbidity. It is mediated by the P. falciparum erythrocyte membrane protein 1 (PfEMP-1) which is expressed at the surface of infected erythocytes and is linked to both antigenic variation and cytoadherence. The PfEMP-1 protein contains multiple adhesive modules, including the cysteine-rich interdomain region (CIDR). The interaction between CIDRa and CD36 promotes stable adherence of parasitized erythrocytes to endothelial cells. Here we show that a segment within the C-terminal region of CIDRa determines CD36 binding specificity. Antibodies raised against this segment can specifically block the adhesion of various parasite stains to CD36. Thus, small regions of PfEMP-1 that determine binding specificity could form suitable components of an anti-sequestration malaria vaccine effective against different parasite strains. DOCTOR OF PHILOSOPHY (SBS) 2008-09-17T11:41:55Z 2008-09-17T11:41:55Z 2007 2007 Thesis Mo, M. (2007). Studies of the molecules form plasmodium falciparum that mediate pathogenesis. Doctoral thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/6566 10.32657/10356/6566 Nanyang Technological University application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
topic DRNTU::Science::Biological sciences
spellingShingle DRNTU::Science::Biological sciences
Mo, Min
Studies of the molecules form plasmodium falciparum that mediate pathogenesis
description Adhesion of erythrocytes infected by Plasmodium falciparum to receptors of the microvasculature is a major contributor of parasite pathology and morbidity. It is mediated by the P. falciparum erythrocyte membrane protein 1 (PfEMP-1) which is expressed at the surface of infected erythocytes and is linked to both antigenic variation and cytoadherence. The PfEMP-1 protein contains multiple adhesive modules, including the cysteine-rich interdomain region (CIDR). The interaction between CIDRa and CD36 promotes stable adherence of parasitized erythrocytes to endothelial cells. Here we show that a segment within the C-terminal region of CIDRa determines CD36 binding specificity. Antibodies raised against this segment can specifically block the adhesion of various parasite stains to CD36. Thus, small regions of PfEMP-1 that determine binding specificity could form suitable components of an anti-sequestration malaria vaccine effective against different parasite strains.
author2 Julien Lescar
author_facet Julien Lescar
Mo, Min
format Theses and Dissertations
author Mo, Min
author_sort Mo, Min
title Studies of the molecules form plasmodium falciparum that mediate pathogenesis
title_short Studies of the molecules form plasmodium falciparum that mediate pathogenesis
title_full Studies of the molecules form plasmodium falciparum that mediate pathogenesis
title_fullStr Studies of the molecules form plasmodium falciparum that mediate pathogenesis
title_full_unstemmed Studies of the molecules form plasmodium falciparum that mediate pathogenesis
title_sort studies of the molecules form plasmodium falciparum that mediate pathogenesis
publishDate 2008
url https://hdl.handle.net/10356/6566
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