Human carcinoembryonic antigen and biliary glycoprotein can serve as mouse hepatitis virus receptors

Chen, D. S.; Asanaka, Miyuki; Chen, F. S.; Shively, J. E.; Lai, Michael M. C.

doi:10.1128/jvi.71.2.1688-1691.1997

Cited by 33 publications

(28 citation statements)

References 25 publications

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“…Delayed brain tumor cells selected for high-level expression of the MHV receptor carcino-embryonic antigen cell adhesion molecule-1 (DBT-9) (Chen et al, 1997;Hirano et al, 1976;Yount et al, 2002) and baby hamster kidney-21 cells expressing the MHV receptor (BHK-MHVR) (Chen et al, 1997;Yount et al, 2002) were grown in Dulbecco's modified Eagle medium (DMEM) (Gibco) that was supplemented with 10% heat-inactivated fetal calf serum (FCS) (Sigma) for all experiments. Medium for BHK-MHVR cells was supplemented with G418 (800 Ag/ ml) to select for cells expressing the MHV receptor.…”

Section: Cells and Antiseramentioning

confidence: 99%

Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replication

Brockway

Denison

2005

Virology

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Despite ongoing research investigating mechanisms of coronavirus replication, functions of many viral nonstructural proteins (nsps) remain unknown. In the current study, a reverse genetic approach was used to define the role of the 28-kDa amino-terminal product (nsp1) of the gene 1 polyprotein during replication of the coronavirus murine hepatitis virus (MHV) in cell culture. To determine whether nsp1 is required for MHV replication and to identify residues critical for protein function, mutant viruses that contained deletions or point mutations within the nsp1-coding region were generated and assayed for defects in viral replication, viral protein expression, protein localization, and RNA synthesis. The results demonstrated that the carboxy-terminal half of nsp1 (residues K(124) through L(241)) was dispensable for virus replication in culture but was required for efficient proteolytic cleavage of nsp1 from the gene 1 polyprotein and for optimal viral replication. Furthermore, whereas deletion of nsp1 residues amino-terminal to K(124) failed to produce infectious virus, point mutagenesis of the nsp1 amino-terminus allowed recovery of several mutants with altered replication and RNA synthesis. This study identifies nsp1 residues important for protein processing, viral RNA synthesis, and viral replication.

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Section: Cells and Antiseramentioning

confidence: 99%

Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replication

Brockway

Denison

2005

Virology

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“…The viral spike glycoprotein can be cleaved into S1 and S2 domains (Bergeron et al, 2005;Du et al, 2007;Follis et al, 2006;Huang et al, 2006;Jackwood et al, 2001;Kawase et al, 2009;Watanabe et al, 2008;Yamada et al, 1998). The S1 domain of the viral spike protein dictates tropism and is responsible for mediating receptor binding (Chen et al, 1997;Han et al, 2007;Hensley and Baric, 1998;Hofmann et al, 2006;Lewicki and Gallagher, 2002;Li et al, 2003Li et al, , 2007Schultze et al, 1996;Thorp and Gallagher, 2004;Wentworth and Holmes, 2001). The S2 domain is responsible for mediating membrane fusion between the virus and host cell, with strong sequence conservation within the family (Bosch et al, 2004;Chu et al, 2006)-hence the mechanics of fusion can be expected to be conserved across the Coronaviridae.…”

Section: Introductionmentioning

confidence: 99%

SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion

2009

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The S2 domain of the coronavirus spike (S) protein is known to be responsible for mediating membrane fusion. In addition to a well-recognized cleavage site at the S1–S2 boundary, a second proteolytic cleavage site has been identified in the severe acute respiratory syndrome coronavirus (SARS-CoV) S2 domain (R797). C terminal to this S2 cleavage site is a conserved region flanked by cysteine residues C822 and C833. Here, we investigated the importance of this well conserved region for SARS-CoV S-mediated fusion activation. We show that the residues between C822-C833 are well conserved across all coronaviruses. Mutagenic analysis of SARS-CoV S, combined with cell–cell fusion and pseudotyped virion infectivity assays, showed a critical role for the core-conserved residues C822, D830, L831, and C833. Based on available predictive models, we propose that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.

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“…B cells were tested for the ability to lyse cells infected with the nonfusogenic MHV-2 strain (Tsai et al, 1999), which utilizes the identical MHV-R (Chen et al, 1997), to confirm a requirement for S-protein-mediated cell-cell fusion (Wysocka et al, 1989). In contrast to cells infected with either fusogenic JHMV or MHV-A59, cells infected with MHV-2 were resistant to B-cell-mediated lysis (Fig.…”

Section: S Protein Fusion-dependent B Cell Cytolysismentioning

confidence: 99%

B-Cell-Mediated Lysis of Cells Infected with the Neurotropic JHM Strain of Mouse Hepatitis Virus

et al. 2001

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Cells expressing the spike (S) glycoprotein of the neurotropic JHM strain (JHMV) of mouse hepatitis virus (MHV) are susceptible to lysis by B cells derived from naïve mice, including B cells from perforin-deficient mice. Cytolysis requires interaction of the virus receptor and the viral S glycoprotein, is independent of other viral-induced components, and is not a unique property of B cells. Neutralizing anti-S-protein monoclonal antibodies (mAb) and a mAb specific for the viral receptor inhibit lysis. However, cells infected with an MHV strain unable to induce cell-cell fusion are resistant to lysis and lysis of JHMV-infected cells is inhibited by an anti-S-protein nonneutralizing mAb which prevents S-protein-mediated cell fusion. These data suggest that B cells may function as antibody-independent innate immune response during JHMV infection in vivo.

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Human carcinoembryonic antigen and biliary glycoprotein can serve as mouse hepatitis virus receptors

Abstract: Receptors for murine coronavirus mouse hepatitis virus (MHV) are members of the murine carcinoembryonic antigen (CEA) gene family. Since MHV can also infect primates and cause central nervous system lesions (G. F.

Cited by 33 publications

References 25 publications

Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replication

Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replication

SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion

B-Cell-Mediated Lysis of Cells Infected with the Neurotropic JHM Strain of Mouse Hepatitis Virus

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