The duffy-binding-like domain 1 of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a heparan sulfate ligand that requires 12 mers for binding.
Identifieur interne : 003614 ( Main/Exploration ); précédent : 003613; suivant : 003615The duffy-binding-like domain 1 of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a heparan sulfate ligand that requires 12 mers for binding.
Auteurs : A. Barragan [Suède] ; V. Fernandez ; Q. Chen ; A. Von Euler ; M. Wahlgren ; D. SpillmannSource :
- Blood [ 0006-4971 ] ; 2000.
Descripteurs français
- KwdFr :
- Animaux, Antigènes de protozoaire (), Antigènes de protozoaire (isolement et purification), Antigènes de protozoaire (sang), Chromatographie d'affinité, Cinétique, Humains, Héparine (métabolisme), Héparitine sulfate (métabolisme), Membrane érythrocytaire (parasitologie), Membrane érythrocytaire (physiologie), Membrane érythrocytaire (ultrastructure), Plasmodium falciparum (physiologie), Plasmodium falciparum (ultrastructure), Protéines de protozoaire (), Protéines de protozoaire (isolement et purification), Protéines de protozoaire (sang), Sites de fixation.
- MESH :
- isolement et purification : Antigènes de protozoaire, Protéines de protozoaire.
- métabolisme : Héparine, Héparitine sulfate.
- parasitologie : Membrane érythrocytaire.
- physiologie : Membrane érythrocytaire, Plasmodium falciparum.
- sang : Antigènes de protozoaire, Protéines de protozoaire.
- Animaux, Antigènes de protozoaire, Chromatographie d'affinité, Cinétique, Humains, Membrane érythrocytaire, Plasmodium falciparum, Protéines de protozoaire, Sites de fixation.
English descriptors
- KwdEn :
- Animals, Antigens, Protozoan (blood), Antigens, Protozoan (chemistry), Antigens, Protozoan (isolation & purification), Binding Sites, Chromatography, Affinity, Erythrocyte Membrane (parasitology), Erythrocyte Membrane (physiology), Erythrocyte Membrane (ultrastructure), Heparin (metabolism), Heparitin Sulfate (metabolism), Humans, Kinetics, Plasmodium falciparum (physiology), Plasmodium falciparum (ultrastructure), Protozoan Proteins (blood), Protozoan Proteins (chemistry), Protozoan Proteins (isolation & purification).
- MESH :
- chemical , blood : Antigens, Protozoan, Protozoan Proteins.
- chemical , chemistry : Antigens, Protozoan, Protozoan Proteins.
- chemical , isolation & purification : Antigens, Protozoan, Protozoan Proteins.
- chemical , metabolism : Heparin, Heparitin Sulfate.
- parasitology : Erythrocyte Membrane.
- physiology : Erythrocyte Membrane, Plasmodium falciparum.
- ultrastructure : Erythrocyte Membrane, Plasmodium falciparum.
- Animals, Binding Sites, Chromatography, Affinity, Humans, Kinetics.
Abstract
The Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), present on the surfaces of parasitized red blood cells (pRBC), mediates rosetting, a virulent phenotype. Here, we show that pRBC specifically bind heparan sulfate (HS) and heparin onto their surfaces and that the rosetting ligand PfEMP1 specifically adheres to heparin-Sepharose when extracted from the surfaces of radioiodinated infected RBC. An analysis of the binding properties of the different regions of PfEMP1 provides evidence that the Duffy-binding-like domain-1 (DBL-1) is the predominant ligand involved in HS and heparin binding. Soluble DBL-1 requires a minimal heparin fragment size of a 12-mer ( approximately 4 kd) for binding and is critically dependent on N-sulfation. A 12-mer is also the minimal heparin fragment that disrupts naturally formed rosettes. DBL-1 binds specifically to erythrocytes and also to HS from endothelial cells and human aorta but not to chondroitin sulfate A, suggesting that different PfEMP1s mediate adhesion to distinct glycosaminoglycans in individual malaria parasites. Present data suggest that HS on endothelial cells may also be involved in the sequestration of pRBC. Elucidation of these binding mechanisms opens up new possibilities for therapeutic strategies targeting adhesive interactions of pRBC.
PubMed: 10828049
Affiliations:
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Le document en format XML
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Barragan</name><affiliation wicri:level="3"><nlm:affiliation>Microbiology and Tumor Biology Center, Karolinska Institutet and Swedish Institute for Infectious Disease Control, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Microbiology and Tumor Biology Center, Karolinska Institutet and Swedish Institute for Infectious Disease Control, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Fernandez, V" sort="Fernandez, V" uniqKey="Fernandez V" first="V" last="Fernandez">V. Fernandez</name></author><author><name sortKey="Chen, Q" sort="Chen, Q" uniqKey="Chen Q" first="Q" last="Chen">Q. Chen</name></author><author><name sortKey="Von Euler, A" sort="Von Euler, A" uniqKey="Von Euler A" first="A" last="Von Euler">A. Von Euler</name></author><author><name sortKey="Wahlgren, M" sort="Wahlgren, M" uniqKey="Wahlgren M" first="M" last="Wahlgren">M. Wahlgren</name></author><author><name sortKey="Spillmann, D" sort="Spillmann, D" uniqKey="Spillmann D" first="D" last="Spillmann">D. Spillmann</name></author></analytic><series><title level="j">Blood</title><idno type="ISSN">0006-4971</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antigens, Protozoan (blood)</term><term>Antigens, Protozoan (chemistry)</term><term>Antigens, Protozoan (isolation & purification)</term><term>Binding Sites</term><term>Chromatography, Affinity</term><term>Erythrocyte Membrane (parasitology)</term><term>Erythrocyte Membrane (physiology)</term><term>Erythrocyte Membrane (ultrastructure)</term><term>Heparin (metabolism)</term><term>Heparitin Sulfate (metabolism)</term><term>Humans</term><term>Kinetics</term><term>Plasmodium falciparum (physiology)</term><term>Plasmodium falciparum (ultrastructure)</term><term>Protozoan Proteins (blood)</term><term>Protozoan Proteins (chemistry)</term><term>Protozoan Proteins (isolation & purification)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigènes de protozoaire ()</term><term>Antigènes de protozoaire (isolement et purification)</term><term>Antigènes de protozoaire (sang)</term><term>Chromatographie d'affinité</term><term>Cinétique</term><term>Humains</term><term>Héparine (métabolisme)</term><term>Héparitine sulfate (métabolisme)</term><term>Membrane érythrocytaire (parasitologie)</term><term>Membrane érythrocytaire (physiologie)</term><term>Membrane érythrocytaire (ultrastructure)</term><term>Plasmodium falciparum (physiologie)</term><term>Plasmodium falciparum (ultrastructure)</term><term>Protéines de protozoaire ()</term><term>Protéines de protozoaire (isolement et purification)</term><term>Protéines de protozoaire (sang)</term><term>Sites de fixation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Antigens, Protozoan</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antigens, Protozoan</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Antigens, Protozoan</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Heparin</term><term>Heparitin Sulfate</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Antigènes de protozoaire</term><term>Protéines de protozoaire</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Héparine</term><term>Héparitine sulfate</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Membrane érythrocytaire</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Erythrocyte Membrane</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Membrane érythrocytaire</term><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Erythrocyte Membrane</term><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="sang" xml:lang="fr"><term>Antigènes de protozoaire</term><term>Protéines de protozoaire</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Erythrocyte Membrane</term><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Chromatography, Affinity</term><term>Humans</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Antigènes de protozoaire</term><term>Chromatographie d'affinité</term><term>Cinétique</term><term>Humains</term><term>Membrane érythrocytaire</term><term>Plasmodium falciparum</term><term>Protéines de protozoaire</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), present on the surfaces of parasitized red blood cells (pRBC), mediates rosetting, a virulent phenotype. Here, we show that pRBC specifically bind heparan sulfate (HS) and heparin onto their surfaces and that the rosetting ligand PfEMP1 specifically adheres to heparin-Sepharose when extracted from the surfaces of radioiodinated infected RBC. An analysis of the binding properties of the different regions of PfEMP1 provides evidence that the Duffy-binding-like domain-1 (DBL-1) is the predominant ligand involved in HS and heparin binding. Soluble DBL-1 requires a minimal heparin fragment size of a 12-mer ( approximately 4 kd) for binding and is critically dependent on N-sulfation. A 12-mer is also the minimal heparin fragment that disrupts naturally formed rosettes. DBL-1 binds specifically to erythrocytes and also to HS from endothelial cells and human aorta but not to chondroitin sulfate A, suggesting that different PfEMP1s mediate adhesion to distinct glycosaminoglycans in individual malaria parasites. Present data suggest that HS on endothelial cells may also be involved in the sequestration of pRBC. Elucidation of these binding mechanisms opens up new possibilities for therapeutic strategies targeting adhesive interactions of pRBC.</div></front></TEI><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Chen, Q" sort="Chen, Q" uniqKey="Chen Q" first="Q" last="Chen">Q. Chen</name><name sortKey="Fernandez, V" sort="Fernandez, V" uniqKey="Fernandez V" first="V" last="Fernandez">V. Fernandez</name><name sortKey="Spillmann, D" sort="Spillmann, D" uniqKey="Spillmann D" first="D" last="Spillmann">D. Spillmann</name><name sortKey="Von Euler, A" sort="Von Euler, A" uniqKey="Von Euler A" first="A" last="Von Euler">A. Von Euler</name><name sortKey="Wahlgren, M" sort="Wahlgren, M" uniqKey="Wahlgren M" first="M" last="Wahlgren">M. Wahlgren</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Barragan, A" sort="Barragan, A" uniqKey="Barragan A" first="A" last="Barragan">A. Barragan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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