Source:http://linkedlifedata.com/resource/pubmed/id/20220119
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
22
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pubmed:dateCreated |
2010-6-4
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pubmed:abstractText |
During erythrocyte invasion, Plasmodium falciparum merozoites use multiple receptor-ligand interactions in a series of coordinated events, but current knowledge of these interactions is limited. Using real-time imaging of invasion, we established that heparin-like molecules block early, and essential, events in erythrocyte invasion by merozoites. All P falciparum isolates tested, and parasites using different invasion pathways were inhibited to comparable levels. Furthermore, it was not possible to select for heparin-resistant parasites. Heparin-like molecules occur naturally on the surface of human erythrocytes, where they may act as receptors for binding of merozoite surface proteins. Consistent with this, we demonstrated that MSP1-42, a processed form of merozoite surface protein 1 (MSP1) involved in invasion, bound heparin in a specific manner; furthermore, binding was observed with the secondary processing fragment MSP1-33, but not MSP1-19. We defined key structural requirements of heparin-like molecules for invasion inhibition and interactions with MSP1-42. Optimal activity required a degree of sulfation more than or equal to 2, disulfation of the N-acetylglucosamine or hexuronic acid residue, and a minimum chain length of 6 monosaccharides. These findings have significant implications for understanding P falciparum invasion of erythrocytes and the development of novel therapeutics and vaccines.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1528-0020
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
3
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pubmed:volume |
115
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4559-68
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pubmed:meshHeading |
pubmed-meshheading:20220119-Animals,
pubmed-meshheading:20220119-Binding Sites,
pubmed-meshheading:20220119-Erythrocytes,
pubmed-meshheading:20220119-Heparin,
pubmed-meshheading:20220119-Host-Parasite Interactions,
pubmed-meshheading:20220119-Humans,
pubmed-meshheading:20220119-Merozoite Surface Protein 1,
pubmed-meshheading:20220119-Merozoites,
pubmed-meshheading:20220119-Molecular Structure,
pubmed-meshheading:20220119-Peptide Fragments,
pubmed-meshheading:20220119-Plasmodium falciparum,
pubmed-meshheading:20220119-Protein Binding,
pubmed-meshheading:20220119-Protein Processing, Post-Translational,
pubmed-meshheading:20220119-Receptors, Cell Surface
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pubmed:year |
2010
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pubmed:articleTitle |
Interactions with heparin-like molecules during erythrocyte invasion by Plasmodium falciparum merozoites.
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pubmed:affiliation |
Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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