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Article: The C-terminal segment of the cysteine-rich interdomain of Plasmodium falciparum erythrocyte membrane protein 1 determines CD36 binding and elicits antibodies that inhibit adhesion of parasite-infected erythrocytes

TitleThe C-terminal segment of the cysteine-rich interdomain of Plasmodium falciparum erythrocyte membrane protein 1 determines CD36 binding and elicits antibodies that inhibit adhesion of parasite-infected erythrocytes
Authors
Issue Date2008
Citation
Infection And Immunity, 2008, v. 76 n. 5, p. 1837-1847 How to Cite?
AbstractAttachment of erythrocytes infected by Plasmodium falciparum to receptors of the microvasculature is a major contributor to the pathology and morbidity associated with malaria. Adhesion is mediated by the P. falciparum erythrocyte membrane protein 1 (PfEMP-1), which is expressed at the surface of infected erythrocytes and is linked to both antigenic variation and cytoadherence. PfEMP-1 contains multiple adhesive modules, including the Duffy binding-like domain and the cysteine-rich interdomain region (CIDR). The interaction between CIDRα and CD36 promotes stable adherence of parasitized erythrocytes to endothelial cells. Here we show that a segment within the C-terminal region of CIDRα determines CD36 binding specificity. Antibodies raised against this segment can specifically block the adhesion to CD36 of erythrocytes infected with various parasite strains. Thus, small regions of PfEMP-1 that determine binding specificity could form suitable components of an antisequestration malaria vaccine effective against different parasite strains. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/171763
ISSN
2015 Impact Factor: 3.603
2015 SCImago Journal Rankings: 2.342
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMo, Men_US
dc.contributor.authorHooi, CLen_US
dc.contributor.authorKotaka, Men_US
dc.contributor.authorNiang, Men_US
dc.contributor.authorGao, Xen_US
dc.contributor.authorIyer, JKen_US
dc.contributor.authorLescar, Jen_US
dc.contributor.authorPreiser, Pen_US
dc.date.accessioned2012-10-30T06:16:52Z-
dc.date.available2012-10-30T06:16:52Z-
dc.date.issued2008en_US
dc.identifier.citationInfection And Immunity, 2008, v. 76 n. 5, p. 1837-1847en_US
dc.identifier.issn0019-9567en_US
dc.identifier.urihttp://hdl.handle.net/10722/171763-
dc.description.abstractAttachment of erythrocytes infected by Plasmodium falciparum to receptors of the microvasculature is a major contributor to the pathology and morbidity associated with malaria. Adhesion is mediated by the P. falciparum erythrocyte membrane protein 1 (PfEMP-1), which is expressed at the surface of infected erythrocytes and is linked to both antigenic variation and cytoadherence. PfEMP-1 contains multiple adhesive modules, including the Duffy binding-like domain and the cysteine-rich interdomain region (CIDR). The interaction between CIDRα and CD36 promotes stable adherence of parasitized erythrocytes to endothelial cells. Here we show that a segment within the C-terminal region of CIDRα determines CD36 binding specificity. Antibodies raised against this segment can specifically block the adhesion to CD36 of erythrocytes infected with various parasite strains. Thus, small regions of PfEMP-1 that determine binding specificity could form suitable components of an antisequestration malaria vaccine effective against different parasite strains. Copyright © 2008, American Society for Microbiology. All Rights Reserved.en_US
dc.languageengen_US
dc.relation.ispartofInfection and Immunityen_US
dc.titleThe C-terminal segment of the cysteine-rich interdomain of Plasmodium falciparum erythrocyte membrane protein 1 determines CD36 binding and elicits antibodies that inhibit adhesion of parasite-infected erythrocytesen_US
dc.typeArticleen_US
dc.identifier.emailKotaka, M:masayo@hku.hken_US
dc.identifier.authorityKotaka, M=rp00293en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1128/IAI.00480-07en_US
dc.identifier.pmid18299339-
dc.identifier.scopuseid_2-s2.0-42949172481en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-42949172481&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume76en_US
dc.identifier.issue5en_US
dc.identifier.spage1837en_US
dc.identifier.epage1847en_US
dc.identifier.isiWOS:000255267200005-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMo, M=24401670000en_US
dc.identifier.scopusauthoridHooi, CL=24174172500en_US
dc.identifier.scopusauthoridKotaka, M=6604073578en_US
dc.identifier.scopusauthoridNiang, M=9632395100en_US
dc.identifier.scopusauthoridGao, X=7403873318en_US
dc.identifier.scopusauthoridIyer, JK=13405437100en_US
dc.identifier.scopusauthoridLescar, J=6603844493en_US
dc.identifier.scopusauthoridPreiser, P=7004076971en_US
dc.identifier.citeulike6973867-

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