Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane
| Autor: | Gloria Sánchez, M. Isabel Costafreda, Rosa M. Pintó, Lluís Aragonès, Albert Bosch, Enric Ribes |
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| Rok vydání: | 2004 |
| Předmět: |
Hemagglutination
medicine.drug_class viruses Immunology In Vitro Techniques Monoclonal antibody Antibodies Viral Microbiology Virus Virology medicine Glycophorin Humans Glycophorins Binding site Viral Structural Proteins Binding Sites biology Erythrocyte Membrane virus diseases biochemical phenomena metabolism and nutrition digestive system diseases Virus-Cell Interactions Red blood cell medicine.anatomical_structure Capsid Insect Science biology.protein Receptors Virus Capsid Proteins Hepatitis A virus Antibody |
| Zdroj: | Journal of virology. 78(18) |
| ISSN: | 0022-538X |
| Popis: | Hepatitis A virus (HAV) has previously been reported to agglutinate human red blood cells at acidic pHs. Treatment of erythrocytes with different enzymes and chemical reagents indicated that HAV attachment is mediated through an interaction with sialylglycoproteins. HAV hemagglutination could be blocked by incubating the virus with glycophorin A, indicating that this sialylglycoprotein is the erythrocyte receptor. The number of receptors used was estimated to be around 500 per cell. At the same time, HAV-induced hemagglutination could also be blocked by either monoclonal antibody H7C27 or an anti-VP3(102-121) ascitic fluid, indicating that lysine 221 of VP1 and the surrounding VP3 residues lining the capsid pit are involved in HAV binding to erythrocytes. |
| Databáze: | OpenAIRE |
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