Binding of Plasmodium falciparum 175-kilodalton erythrocyte binding antigen and invasion of murine erythrocytes requires N-acetylneuraminic acid but not its O-acetylated form
| Autor: | Peter Palese, Roland Schauer, P. A. Orlandi, Russell J. Howard, J. David Haynes, Louis H. Miller, F W Klotz, Gerd Reuter, Stuart J. Cohen |
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| Rok vydání: | 1992 |
| Předmět: |
EBA-175
175-kDa erythrocyte binding antigen Erythrocytes Neu5 9Ac2 9-O-acetyl-N-acetylneuraminic acid Plasmodium falciparum Red cell Protozoan Proteins Antigens Protozoan Biology Sialidase Article Mice chemistry.chemical_compound Antigen Cell surface receptor parasitic diseases medicine Animals Neu5Gc N-glycoloylneuraminic acid Molecular Biology Binding Sites Ligand (biochemistry) biology.organism_classification Sialic acid Neu5Ac N-acetylneuraminic acid Mice Inbred C57BL Red blood cell medicine.anatomical_structure Biochemistry chemistry Mice Inbred DBA Sialic Acids Parasitology Carrier Proteins Merozoite N-Acetylneuraminic acid Receptor |
| Zdroj: | Molecular and Biochemical Parasitology |
| ISSN: | 0166-6851 |
| Popis: | Sialic acid on human erythrocytes is involved in invasion by the human malaria parasite, Plasmodium falciparum. Mouse erythrocytes were used as a reagent to explore the question of whether erythrocyte sialic acid functions as a nonspecific negative charge or whether the sialic acid is a necessary structural part of the receptor for merozoites. Human erythrocytes contain N-acetylneuraminic acid (Neu5Ac), whereas mouse erythrocytes, which are also invaded by P. falciparum merozoites, contain 9-O-acetyl-N-acetylneuraminic acid (Neu5,9Ac2) and N-glycoloylneuraminic acid (Neu5Gc), in addition to Neu5Ac. We compared the effects of sialidase and influenza C virus esterase treatments of mouse erythrocytes on invasion and the binding of a 175-kDa P. falciparum protein (EBA-175), a sialic acid-dependent malaria ligand implicated in the invasion process. Sialidase-treated mouse erythrocytes were refractory to invasion by P. falciparum merozoites and failed to bind EBA-175. Influenza C virus esterase, which converts Neu5,9Ac2 to Neu5Ac, increased both invasion efficiency and EBA-175 binding to mouse erythrocytes. Thus, the parasite and EBA-175 discriminate between Neu5Ac and Neu5,9Ac2, that is, the C-9 acetyl group interferes with EBA-175 binding and invasion by P. falciparum merozoites. This indicates that sialic acid is part of a receptor for invasion. |
| Databáze: | OpenAIRE |
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