Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane.
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.
Department of Microbiology, University of Barcelona, Av. Diagonal 645, 08028 Barcelona, Spain.
Glòria
G
Sánchez
Lluís
L
Aragonès
M Isabel
MI
Costafreda
Enric
E
Ribes
Albert
A
Bosch
Rosa M
RM
Pintó
D000914:Antibodies, Viral; D001665:Binding Sites; D036022:Capsid Proteins / Q000737:chemistry / Q000276:immunology / Q000502:physiology*; D004910:Erythrocyte Membrane / Q000502:physiology* / Q000821:virology*; D006021:Glycophorins / Q000502:physiology*; D006384:Hemagglutination; D030041:Hepatitis A virus / Q000276:immunology / Q000472:pathogenicity* / Q000502:physiology; D006801:Humans; D066298:In Vitro Techniques; D011991:Receptors, Virus / Q000502:physiology; D015678:Viral Structural Proteins / Q000737:chemistry / Q000276:immunology / Q000502:physiology
D000914:Antibodies, Viral; D036022:Capsid Proteins; D006021:Glycophorins; D011991:Receptors, Virus; C096539:VP1 protein, hepatitis A virus; D015678:Viral Structural Proteins