Literature DB >> 15331714

Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane.

Glòria Sánchez1, Lluís Aragonès, M Isabel Costafreda, Enric Ribes, Albert Bosch, Rosa M Pintó.   

Abstract

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. Copyright 2004 American Society for Microbiology

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Year:  2004        PMID： 15331714      PMCID： PMC514964          DOI： 10.1128/JVI.78.18.9807-9813.2004

Source DB:  PubMed          Journal:  J Virol        ISSN： 0022-538X            Impact factor:   5.103


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