A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytes

The recognition and invasion of human erythrocytes by the most lethal malaria parasite Plasmodium falciparum is dependent on multiple ligand-receptor interactions. Members of the erythrocyte binding-like (ebl) family, including the erythrocyte binding antigen-175 (EBA-175), are responsible for high...

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Bibliographic Details
Published in:The Journal of biological chemistry 2003-04, Vol.278 (16), p.14480-14486
Main Authors: Gilberger, Tim-Wolf, Thompson, Jennifer K, Triglia, Tony, Good, Robert T, Duraisingh, Manoj T, Cowman, Alan F
Format: Article
Language:English
Subjects:
Animals
Antigens - metabolism
Antigens, Protozoan - chemistry
Antigens, Protozoan - metabolism
Antigens, Surface
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Chymotrypsin - pharmacology
Electrophoresis, Polyacrylamide Gel
Erythrocytes - immunology
Erythrocytes - metabolism
Erythrocytes - parasitology
Humans
Immunoblotting
Ligands
Microscopy, Fluorescence
Models, Genetic
Phenotype
Plasmids - metabolism
Plasmodium falciparum - metabolism
Protein Binding
Protein Structure, Tertiary
Protozoan Proteins - chemistry
Protozoan Proteins - metabolism
Recombination, Genetic
Sialoglycoproteins - chemistry
Time Factors
Transfection
Trypsin - pharmacology
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Summary:The recognition and invasion of human erythrocytes by the most lethal malaria parasite Plasmodium falciparum is dependent on multiple ligand-receptor interactions. Members of the erythrocyte binding-like (ebl) family, including the erythrocyte binding antigen-175 (EBA-175), are responsible for high affinity binding to glycoproteins on the surface of the erythrocyte. Here we describe a paralogue of EBA-175 and show that this protein (EBA-181/JESEBL) binds in a sialic acid-dependent manner to erythrocytes. EBA-181 is expressed at the same time as EBA-175 and co-localizes with this protein in the microneme organelles of asexual stage parasites. The receptor binding specificity of EBA-181 to erythrocytes differs from other members of the ebl family and is trypsin-resistant and chymotrypsin-sensitive. Furthermore, using glycophorin B-deficient erythrocytes we show that binding of EBA-181 is not dependent on this sialoglycoprotein. The level of expression of EBA-181 differs among parasite lines, and the importance of this ligand for invasion appears to be strain-dependent as the EBA-181 gene can be disrupted in W2mef parasites, without affecting the invasion phenotype, but cannot be targeted in 3D7 parasites.
ISSN:0021-9258
DOI:10.1074/jbc.M211446200