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rdf:type |
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lifeskim:mentions |
umls-concept:C0013879,
umls-concept:C0014792,
umls-concept:C0032154,
umls-concept:C0678594,
umls-concept:C1269955,
umls-concept:C1514562,
umls-concept:C1704788,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2699153
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2003-8-7
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pubmed:abstractText |
Plasmodium vivax and P. knowlesi use the Duffy antigen as a receptor to invade human erythrocytes. Duffy-binding ligands belong to a family of erythrocyte-binding proteins that bind erythrocyte receptors to mediate invasion. Receptor-binding domains in erythrocyte-binding proteins lie in conserved cysteine-rich regions called Duffy-binding-like domains. In the present study, we report an analysis of the overall three-dimensional architecture of P. vivax and P. knowlesi Duffy-binding domains based on mild proteolysis and supportive-functional assays. Our proteolysis experiments indicate that these domains are built of two distinct subdomains. The N-terminal region from Cys-1-4 (C1-C4) forms a stable non-functional subdomain. The region spanning C5-C12 forms another subdomain, which is capable of binding Duffy antigen. These subdomains are joined by a protease-sensitive linker. Results from deletion constructs, designed for expression of truncated proteins on COS cell surface, show that regions containing C5-C8 of the Duffy-binding domains are sufficient for the binding receptor. Therefore the central region of Duffy-binding domains, which is flanked by two non-functional regions, is responsible for receptor recognition. Moreover, the minimal Duffy-binding region identified here is capable of folding into a functionally competent module. These studies pave the way for understanding the architecture of Duffy-binding domains and their interactions with host receptors.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-10535993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-10570199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-10677532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-10880521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-11279211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-11309486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-11378038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-1145213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-11985860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-12461087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-12469115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-12556470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-13650640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-1496004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-2229177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-2452897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-3901257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-7541722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-7606775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-7606788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-7689250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-778616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-8009226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-8046329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-9230440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12775212-9419207
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Protozoan,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Duffy antigen binding protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
374
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
193-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12775212-Animals,
pubmed-meshheading:12775212-Antigens, Protozoan,
pubmed-meshheading:12775212-Base Sequence,
pubmed-meshheading:12775212-Binding Sites,
pubmed-meshheading:12775212-Cell Adhesion Molecules,
pubmed-meshheading:12775212-Cloning, Molecular,
pubmed-meshheading:12775212-DNA Primers,
pubmed-meshheading:12775212-Erythrocytes,
pubmed-meshheading:12775212-Escherichia coli,
pubmed-meshheading:12775212-Humans,
pubmed-meshheading:12775212-Molecular Sequence Data,
pubmed-meshheading:12775212-Mutagenesis,
pubmed-meshheading:12775212-Peptide Fragments,
pubmed-meshheading:12775212-Plasmodium knowlesi,
pubmed-meshheading:12775212-Plasmodium vivax,
pubmed-meshheading:12775212-Polymerase Chain Reaction,
pubmed-meshheading:12775212-Protozoan Proteins,
pubmed-meshheading:12775212-Receptors, Cell Surface,
pubmed-meshheading:12775212-Recombinant Proteins,
pubmed-meshheading:12775212-Sequence Deletion,
pubmed-meshheading:12775212-Trypsin
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pubmed:year |
2003
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pubmed:articleTitle |
Definition of structural elements in Plasmodium vivax and P. knowlesi Duffy-binding domains necessary for erythrocyte invasion.
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pubmed:affiliation |
Malaria Research Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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