Strategies for the identification of icosahedral virus receptors.

Bass, Dorsey; Greenberg, Harry B.

doi:10.1172/jci115575

Cited by 24 publications

(12 citation statements)

References 87 publications

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“…Viral attachment is the first step in virus infection (41). The distribution of a virus receptor mainly determines the cell and tissue tropism of the virus (1,11) and the site of pathology associated with infection (9,26). Thus, study of virus infection at the levels of virus binding, receptor identification, and even uncoating is critical for an understanding of the virus-host cell interactions and pathogenesis of viral disease (24,32).…”

Section: Infectious Bursal Disease Virus (Ibdv) a Member Of Genusmentioning

confidence: 99%

Chicken Heat Shock Protein 90 Is a Component of the Putative Cellular Receptor Complex of Infectious Bursal Disease Virus

Lin

Lai

et al. 2007

J Virol

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Infectious bursal disease virus (IBDV) causes a highly contagious disease in young chicks and leads to significant economic losses in the poultry industry. The capsid protein VP2 of IBDV plays an important role in virus binding and cell recognition. VP2 forms a subviral particle (SVP) with immunogenicity similar to that of the IBDV capsid. In the present study, we first showed that SVP could inhibit IBDV infection to an IBDV-susceptible cell line, DF-1 cells, in a dose-dependent manner. Second, the localizations of the SVP on the surface of DF-1 cells were confirmed by fluorescence microscopy, and the specific binding of the SVP to DF-1 cells occurred in a dose-dependent manner. Furthermore, the attachment of SVP to DF-1 cells was inhibited by an SVP-induced neutralizing monoclonal antibody against IBDV but not by denatured-VP2-induced polyclonal antibodies. Third, the cellular factors in DF-1 cells involved in the attachment of SVP were purified by affinity chromatography using SVP bound on the immobilized Ni 2؉ ions. A dominant factor was identified as being chicken heat shock protein 90 (Hsp90) (cHsp90) by mass spectrometry. Results of biotinylation experiments and indirect fluorescence assays indicated that cHsp90 is located on the surface of DF-1 cells. Virus overlay protein binding assays and far-Western assays also concluded that cHsp90 interacts with IBDV and SVP, respectively. Finally, both Hsp90 and anti-Hsp90 can inhibit the infection of DF-1 cells by IBDV. Taken together, for the first time, our results suggest that cHsp90 is part of the putative cellular receptor complex essential for IBDV entry into DF-1 cells. Infectious bursal disease virus (IBDV), a member of genusAvibirnavirus of the family Birnaviridae, causes a highly contagious disease in young chicks (27). Two serotypes (serotypes 1 and 2) of IBDV have been documented. Serotype 1 showed different degrees of pathogenicity and mortality in chicks, and serotype 2 was avirulent. As with all viruses, IBDV needs to penetrate target cells to cause infection. Chicken B lymphocytes are the primary target for virulent serotype 1 strains of IBDV, and the infection causes a functional loss of the bursa of Fabricius and severe immunodepression. However, other susceptible cells have also been reported (17). Viral attachment is the first step in virus infection (41). The distribution of a virus receptor mainly determines the cell and tissue tropism of the virus (1, 11) and the site of pathology associated with infection (9, 26). Thus, study of virus infection at the levels of virus binding, receptor identification, and even uncoating is critical for an understanding of the virus-host cell interactions and pathogenesis of viral disease (24, 32). Additionally, viral entry and uncoating can serve as targets for the development of antiviral drugs (39,42). Recent advances in the understanding of the viral infection process have made it possible to develop new approaches to block the entry of viruses (31) and to prevent diseases (41). However, the identificatio...

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Section: Infectious Bursal Disease Virus (Ibdv) a Member Of Genusmentioning

confidence: 99%

Chicken Heat Shock Protein 90 Is a Component of the Putative Cellular Receptor Complex of Infectious Bursal Disease Virus

Lin

Lai

et al. 2007

J Virol

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“…Because cellular receptors for other picornaviruses have been characterized by raising monoclonal antibodies (mAbs) against susceptible cells and selecting those capable of blocking infection (Bass and Greenberg, 1992), we decided to use a similar approach to identify cellular receptors for HAV. Here we report that three mAbs directed against the cell surface protected African green monkey kidney (AGMK) cells against HAV infection.…”

Section: Introductionmentioning

confidence: 99%

Identification of a surface glycoprotein on African green monkey kidney cells as a receptor for hepatitis A virus.

et al. 1996

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Very little is known about the mechanism of cell entry of hepatitis A virus (HAV), and the identification of cellular receptors for this picornavirus has been elusive. Here we describe the molecular cloning of a cellular receptor for HAV using protective monoclonal antibodies raised against susceptible African green monkey kidney (AGMK) cells as probes. Monoclonal antibodies 190/4, 235/4 and 263/6, which reacted against similar epitopes, specifically protected AGMK cells against HAV infection by blocking the binding of HAV. Expression cloning and nucleotide sequence analysis of the cDNA coding for epitope 190/4 revealed a novel mucin‐like class I integral membrane glycoprotein of 451 amino acids, the HAV cellular receptor 1 (HAVcr‐1). Immunofluorescence analysis indicated that mouse Ltk‐ cells transfected with HAVcr‐1 cDNA gained limited susceptibility to HAV infection, which was blocked by treatment with monoclonal antibody 190/4. Our results demonstrate that the HAVcr‐1 polypeptide is an attachment receptor for HAV and strongly suggest that it is also a functional receptor which mediates HAV infection. This report constitutes the first identification of a cellular receptor for HAV.

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“…In some instances virus tropism is strictly determined by the presence of speci®c receptors that mediate binding and entry (Bai et al, 1993;Dalgleish et al, 1984;Haywood, 1994;Klatzman et al, 1984;Mendelsohn et al, 1989;Philipson et al, 1968;Racaniello, 1990;Tomassini et al, 1989;Weiss, 1993;Weiss and Tailor, 1995;Wickham et al, 1993). In other instances, however, successful entry into a cell is necessary but not suf®cient for virus growth (Atwood, 1991;Bass and Greenberg, 1992;Mei and Wadell, 1995;Rossman, 1994). In these cases, additional permissive factors that interact with viral regulatory elements are required.…”

Section: Introductionmentioning

confidence: 99%

The Human Polyomavirus, Jcv, Does Not Share Receptor Specificity with SV40 on Human Glial Cells

1998

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The initial event in the life cycle of a virus is its interaction with speci®c receptors present on the surface of a cell. Understanding these interactions is important to our understanding of viral tropism and tissue speci®c pathology associated with viral disease. The human polyomavirus, JCV, is the etiological agent of the fatal central nervous system (CNS) demyelinating disease, progressive multifocal leukoencephalopathy (PML). PML is the direct result of JCV infection of oligodendrocytes, the myelin producing cell in the CNS. In vivo, JCV can be detected in oligodendrocytes, astrocytes, lymphoid tissue, and peripheral blood of PML patients. In vitro, JCV infects human glial cells, tonsilar stromal cells, and, to a limited extent, human B lymphocytes. The initial step in infection of cells by JCV is at the level of attachment and entry. A speci®c cell surface receptor for JCV on human glial cells has not been identi®ed. To begin to understand the nature of JCV receptors on human glial cells, large quantities of a previously characterized hybrid JC virus (Mad-1/ SVED) were puri®ed. A direct virus binding assay demonstrated that these highly puri®ed and labeled JCV virions bound to a ®nite number of cellular receptors on human glial cells. A competitive virus binding assay demonstrated that an excess of unlabeled JCV competed with labeled JCV more ef®ciently than did an excess of puri®ed SV40. Furthermore, anti-class I antibodies which inhibited infection of glial cells by SV40 had no signi®cant effect on infection by JCV. These results imply that JCV does not share receptor speci®city with the related polyomavirus, SV40.

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Strategies for the identification of icosahedral virus receptors.

Cited by 24 publications

References 87 publications

Chicken Heat Shock Protein 90 Is a Component of the Putative Cellular Receptor Complex of Infectious Bursal Disease Virus

Chicken Heat Shock Protein 90 Is a Component of the Putative Cellular Receptor Complex of Infectious Bursal Disease Virus

Identification of a surface glycoprotein on African green monkey kidney cells as a receptor for hepatitis A virus.

The Human Polyomavirus, Jcv, Does Not Share Receptor Specificity with SV40 on Human Glial Cells

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