ArticleJournal of virology2001
Neutralization of hepatitis A virus (HAV) by an immunoadhesin containing the cysteine-rich region of HAV cellular receptor-1.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 49 citations in OpenAlex.
- KIM-1: A Non-Invasive Marker for Kidney Injury and Treatment Efficacy in FMF.Mediterranean journal of rheumatology · 2026Article
- Reply to Das et al., "TIM1 (HAVCR1): an Essential 'Receptor' or an 'Accessory Attachment Factor' for Hepatitis A Virus?"Journal of virology · 2019Article
- The Interplay of Viral and Host Factors in Chikungunya Virus Infection: Targets for Antiviral Strategies.Viruses · 2018Review
- HAVCR1 (CD365) and Its Mouse Ortholog Are Functional Hepatitis A Virus (HAV) Cellular Receptors That Mediate HAV Infection.Journal of virology · 2018Article
- Article
- Viral apoptotic mimicry.Nature reviews. Microbiology · 2015Review
- TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine.PLoS pathogens · 2013Article
- Ebola virus glycoprotein Fc fusion protein confers protection against lethal challenge in vaccinated mice.Vaccine · 2011Article
- Conformational changes in the capsid of a calicivirus upon interaction with its functional receptor.Journal of virology · 2010Article
- Picornaviruses.Current topics in microbiology and immunology · 2010Article
- The interaction of hepatitis A virus (HAV) with soluble forms of its cellular receptor 1 (HAVCR1) share the physiological requirements of infectivity in cell culture.Virology journal · 2009Article
- A simple and rapid Hepatitis A Virus (HAV) titration assay based on antibiotic resistance of infected cells: evaluation of the HAV neutralization potency of human immune globulin preparations.Virology journal · 2008Article
- Immunoglobulin A (IgA) is a natural ligand of hepatitis A virus cellular receptor 1 (HAVCR1), and the association of IgA with HAVCR1 enhances virus-receptor interactions.Journal of virology · 2007Article
- Growth of hepatitis A virus in a mouse liver cell line.Journal of virology · 2005Article
- Interactions of foot-and-mouth disease virus with soluble bovine alphaVbeta3 and alphaVbeta6 integrins.Journal of virology · 2004Article
- Capsid region involved in hepatitis A virus binding to glycophorin A of the erythrocyte membrane.Journal of virology · 2004Article
- Alteration of hepatitis A virus (HAV) particles by a soluble form of HAV cellular receptor 1 containing the immunoglobin-and mucin-like regions.Journal of virology · 2003Article
- Mutations conferring resistance to neutralization by a soluble form of the neurotrophin receptor (p75NTR) map outside of the known antigenic sites of the rabies virus glycoprotein.Journal of virology · 2002Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis A virus (HAV) infects African green monkey kidney (AGMK) cells via the HAV cellular receptor-1 (havcr-1), a mucin-like type 1 integral-membrane glycoprotein of unknown natural function. The ectodomain of havcr-1 contains an N-terminal immunoglobulin-like cysteine-rich region (D1), which binds protective monoclonal antibody (MAb) 190/4, followed by an O-glycosylated mucin-like threonine-serine-proline-rich region that extends D1 well above the cell surface. To study the interaction of HAV with havcr-1, we constructed immunoadhesins fusing the hinge and Fc portion of human IgG1 to D1 (D1-Fc) or the ectodomain of the poliovirus receptor (PVR-Fc) and expressed them in CHO cells. These immunoadhesins were secreted to the cell culture medium and purified through protein A-agarose columns. In a solid-phase assay, HAV bound to D1-Fc in a concentration-dependent manner whereas background levels of HAV bound to PVR-Fc. Binding of HAV to D1-Fc was blocked by treatment with MAb 190/4 but not with control MAb M2, which binds to a tag epitope introduced between the D1 and Fc portions of the immunoadhesin. D1-Fc neutralized approximately 1 log unit of the HAV infectivity in AGMK cells, whereas PVR-Fc had no effect in the HAV titers. A similarly poor reduction in HAV titers was observed after treating the same stock of HAV with murine neutralizing MAbs K2-4F2, K3-4C8, and VHA 813. Neutralization of poliovirus by PVR-Fc but not by D1-Fc indicated that the virus-receptor interactions were specific. These results show that D1 is sufficient for binding and neutralization of HAV and provide further evidence that havcr-1 is a functional cellular receptor for HAV.
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