Academic literature on the topic 'MHV-A59'

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Journal articles on the topic "MHV-A59"

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Leparc-Goffart, Isabelle, Susan T. Hingley, Ming Ming Chua, Joanna Phillips, Ehud Lavi, and Susan R. Weiss. "Targeted Recombination within the Spike Gene of Murine Coronavirus Mouse Hepatitis Virus-A59: Q159 Is a Determinant of Hepatotropism." Journal of Virology 72, no. 12 (1998): 9628–36. http://dx.doi.org/10.1128/jvi.72.12.9628-9636.1998.

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ABSTRACT Previous studies of a group of mutants of the murine coronavirus mouse hepatitis virus (MHV)-A59, isolated from persistently infected glial cells, have shown a strong correlation between a Q159L amino acid substitution in the S1 subunit of the spike gene and a loss in the ability to induce hepatitis and demyelination. To determine if Q159L alone is sufficient to cause these altered pathogenic properties, targeted RNA recombination was used to introduce a Q159L amino acid substitution into the spike gene of MHV-A59. Recombination was carried out between the genome of a temperature-sens
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Navas, Sonia, Su-Hun Seo, Ming Ming Chua, et al. "Murine Coronavirus Spike Protein Determines the Ability of the Virus To Replicate in the Liver and Cause Hepatitis." Journal of Virology 75, no. 5 (2001): 2452–57. http://dx.doi.org/10.1128/jvi.75.5.2452-2457.2001.

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ABSTRACT Recombinant mouse hepatitis viruses (MHV) differing only in the spike gene, containing A59, MHV-4, and MHV-2 spike genes in the background of the A59 genome, were compared for their ability to replicate in the liver and induce hepatitis in weanling C57BL/6 mice infected with 500 PFU of each virus by intrahepatic injection. Penn98-1, expressing the MHV-2 spike gene, replicated to high titer in the liver, similar to MHV-2, and induced severe hepatitis with extensive hepatocellular necrosis. SA59R13, expressing the A59 spike gene, replicated to a somewhat lower titer and induced moderate
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Hirai, Asuka, Nobuhisa Ohtsuka, Toshio Ikeda, et al. "Role of Mouse Hepatitis Virus (MHV) Receptor Murine CEACAM1 in the Resistance of Mice to MHV Infection: Studies of Mice with Chimeric mCEACAM1a and mCEACAM1b." Journal of Virology 84, no. 13 (2010): 6654–66. http://dx.doi.org/10.1128/jvi.02680-09.

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ABSTRACT Although most inbred mouse strains are highly susceptible to mouse hepatitis virus (MHV) infection, the inbred SJL line of mice is highly resistant to its infection. The principal receptor for MHV is murine CEACAM1 (mCEACAM1). Susceptible strains of mice are homozygous for the 1a allele of mCeacam1, while SJL mice are homozygous for the 1b allele. mCEACAM1a (1a) has a 10- to 100-fold-higher receptor activity than does mCEACAM1b (1b). To explore the hypothesis that MHV susceptibility is due to the different MHV receptor activities of 1a and 1b, we established a chimeric C57BL/6 mouse (
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Yount, Boyd, Mark R. Denison, Susan R. Weiss, and Ralph S. Baric. "Systematic Assembly of a Full-Length Infectious cDNA of Mouse Hepatitis Virus Strain A59." Journal of Virology 76, no. 21 (2002): 11065–78. http://dx.doi.org/10.1128/jvi.76.21.11065-11078.2002.

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ABSTRACT A novel method was developed to assemble a full-length infectious cDNA of the group II coronavirus mouse hepatitis virus strain A59 (MHV-A59). Seven contiguous cDNA clones that spanned the 31.5-kb MHV genome were isolated. The ends of the cDNAs were engineered with unique junctions and assembled with only the adjacent cDNA subclones, resulting in an intact MHV-A59 cDNA construct of ∼31.5 kb in length. The interconnecting restriction site junctions that are located at the ends of each cDNA are systematically removed during the assembly of the complete full-length cDNA product, allowing
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Hingley, Susan T., Isabelle Leparc-Goffart, and Susan R. Weiss. "The Spike Protein of Murine Coronavirus Mouse Hepatitis Virus Strain A59 Is Not Cleaved in Primary Glial Cells and Primary Hepatocytes." Journal of Virology 72, no. 2 (1998): 1606–9. http://dx.doi.org/10.1128/jvi.72.2.1606-1609.1998.

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ABSTRACT Mouse hepatitis virus strain A59 (MHV-A59) produces meningoencephalitis and severe hepatitis during acute infection. Infection of primary cells derived from the central nervous system (CNS) and liver was examined to analyze the interaction of virus with individual cell types derived from the two principal sites of viral replication in vivo. In glial cell cultures derived from C57BL/6 mice, MHV-A59 produces a productive but nonlytic infection, with no evidence of cell-to-cell fusion. In contrast, in continuously cultured cells, this virus produces a lytic infection with extensive forma
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Gilmore, W., J. Correale, and L. P. Weiner. "Coronavirus induction of class I major histocompatibility complex expression in murine astrocytes is virus strain specific." Journal of Experimental Medicine 180, no. 3 (1994): 1013–23. http://dx.doi.org/10.1084/jem.180.3.1013.

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Neurotropic strains of mouse hepatitis viruses (MHV) such as MHV-A59 (A59) and MHV-4 (JHMV) cause acute and chronic encephalomyelitis and demyelination in susceptible strains of mice and rats. They are widely used as models of human demyelinating diseases such as multiple sclerosis (MS), in which immune mechanisms are thought to participate in the development of lesions in the central nervous system (CNS). The effects of MHV infection on target cell functions in the CNS are not well understood, but A59 has been shown to induce the expression of MHC class I molecules in glial cells after in viv
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Miura, Tanya A., Emily A. Travanty, Lauren Oko, et al. "The Spike Glycoprotein of Murine Coronavirus MHV-JHM Mediates Receptor-Independent Infection and Spread in the Central Nervous Systems of Ceacam1a−/− Mice." Journal of Virology 82, no. 2 (2007): 755–63. http://dx.doi.org/10.1128/jvi.01851-07.

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ABSTRACT The MHV-JHM strain of the murine coronavirus mouse hepatitis virus is much more neurovirulent than the MHV-A59 strain, although both strains use murine CEACAM1a (mCEACAM1a) as the receptor to infect murine cells. We previously showed that Ceacam1a −/− mice are completely resistant to MHV-A59 infection (E. Hemmila et al., J. Virol. 78:10156-10165, 2004). In vitro, MHV-JHM, but not MHV-A59, can spread from infected murine cells to cells that lack mCEACAM1a, a phenomenon called receptor-independent spread. To determine whether MHV-JHM could infect and spread in the brain independent of m
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Zelus, Bruce D., David R. Wessner, Richard K. Williams, et al. "Purified, Soluble Recombinant Mouse Hepatitis Virus Receptor, Bgp1b, and Bgp2 Murine Coronavirus Receptors Differ in Mouse Hepatitis Virus Binding and Neutralizing Activities." Journal of Virology 72, no. 9 (1998): 7237–44. http://dx.doi.org/10.1128/jvi.72.9.7237-7244.1998.

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ABSTRACT Mouse hepatitis virus receptor (MHVR) is a murine biliary glycoprotein (Bgp1a). Purified, soluble MHVR expressed from a recombinant vaccinia virus neutralized the infectivity of the A59 strain of mouse hepatitis virus (MHV-A59) in a concentration-dependent manner. Several anchored murine Bgps in addition to MHVR can also function as MHV-A59 receptors when expressed at high levels in nonmurine cells. To investigate the interactions of these alternative MHVR glycoproteins with MHV, we expressed and purified to apparent homogeneity the extracellular domains of several murine Bgps as solu
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Tsai, Jean C., Bruce D. Zelus, Kathryn V. Holmes, and Susan R. Weiss. "The N-Terminal Domain of the Murine Coronavirus Spike Glycoprotein Determines the CEACAM1 Receptor Specificity of the Virus Strain." Journal of Virology 77, no. 2 (2003): 841–50. http://dx.doi.org/10.1128/jvi.77.2.841-850.2003.

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ABSTRACT Using isogenic recombinant murine coronaviruses expressing wild-type murine hepatitis virus strain 4 (MHV-4) or MHV-A59 spike glycoproteins or chimeric MHV-4/MHV-A59 spike glycoproteins, we have demonstrated the biological functionality of the N-terminus of the spike, encompassing the receptor binding domain (RBD). We have used two assays, one an in vitro liposome binding assay and the other a tissue culture replication assay. The liposome binding assay shows that interaction of the receptor with spikes on virions at 37°C causes a conformational change that makes the virions hydrophob
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Leibowitz, Julian L., Rajiv Srinivasa, Shawn T. Williamson, et al. "Genetic Determinants of Mouse Hepatitis Virus Strain 1 Pneumovirulence." Journal of Virology 84, no. 18 (2010): 9278–91. http://dx.doi.org/10.1128/jvi.00330-10.

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ABSTRACT We report here investigation into the genetic basis of mouse hepatitis virus strain 1 (MHV-1) pneumovirulence. Sequencing of the 3′ one-third of the MHV-1 genome demonstrated that the genetic organization of MHV-1 was similar to that of other strains of MHV. The hemagglutinin esterase (HE) protein was truncated, and reverse transcription-PCR (RT-PCR) studies confirmed previous work that suggested that the MHV-1 HE is a pseudogene. Targeted recombination was used to select chimeric viruses containing either the MHV-1 S gene or genes encoding all of the MHV-1 structural proteins, on an
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Dissertations / Theses on the topic "MHV-A59"

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Eifart, Patricia. "Visualisierung und Charakterisierung der S-Protein vermittelten Fusion von Coronaviren." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2008. http://dx.doi.org/10.18452/15733.

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Die Fusionsreaktion des Coronavirus MHV wird vom S-Protein vermittelt. In der vorliegenden Arbeit wurde der Eintrittsweg von MHV-A59 in Mauszellen untersucht. Die Infektivität kann durch lysosomotrope Substanzen und Inhibitoren der Clathrin-abhängigen Endozytose gehemmt werden. Der Eintritt von MHV-A59 in Mauszellen erfolgt über die Clathrin-abhängige Endozytose und setzt die anschließende Fusion der viralen und zellulären Membran bei niedrigem pH-Wert voraus. Fluoreszenzmikroskopische Studien zur Interaktion fluoreszenzmarkierter MHV-A59 Partikel mit Mauszellen bestätigen, dass MHV-A59 über E
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Book chapters on the topic "MHV-A59"

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Sturman, L. S., C. Eastwood, M. F. Frana, et al. "Temperature-Sensitive Mutants of MHV-A59." In Coronaviruses. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-1280-2_20.

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Lavi, E., L. Kuo, J. A. Haluskey, and P. S. Masters. "Targeted Recombination Between MHV-2 and MHV-A59 to Study Neurotropic Determinants of MHV." In Advances in Experimental Medicine and Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_70.

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Donaldson, Eric F., Amy C. Sims, Damon J. Deming, and Ralph S. Baric. "Mutational Analysis of MHV-A59 Replicase Protein-NSP10." In Advances in Experimental Medicine and Biology. Springer US, 2006. http://dx.doi.org/10.1007/978-0-387-33012-9_9.

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Sims, A. C., X. T. Lu, and M. R. Denison. "Expression, Purification, and Activity of Recombinant MHV-A59 3CLpro." In Advances in Experimental Medicine and Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_17.

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Zelus, Bruce D., David R. Wessner, Gabriela S. Dveksler, and Kathryn V. Holmes. "Neutralization of MHV-A59 by Soluble Recombinant Receptor Glycoproteins." In Advances in Experimental Medicine and Biology. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5331-1_1.

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Denison, Mark R., James C. Kim, and Theodore Ross. "Inhibition of Coronavirus MHV-A59 Replication by Proteinase Inhibitors." In Advances in Experimental Medicine and Biology. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1899-0_64.

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Hughes, Scott A., Pedro J. Bonilla, and Susan R. Weiss. "Identification and Analysis of MHV-A59 P28 Cleavage Site." In Advances in Experimental Medicine and Biology. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1899-0_72.

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Deming, Damon J., Rachel L. Graham, Mark R. Denison, and Ralph S. Baric. "MHV-A59 Orf1a Replicase Protein NSP7-NSP10 Processing in Replication." In Advances in Experimental Medicine and Biology. Springer US, 2006. http://dx.doi.org/10.1007/978-0-387-33012-9_17.

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Lavi, Ehud, Qian Wang, James Gombold, Robyn Sutherland, Yvonne Paterson, and Susan Weiss. "Pathology of MHV-A59 Infection in ß2 Microglobulin Negative Mice." In Advances in Experimental Medicine and Biology. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1899-0_29.

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Bonilla, P. J., J. L. Piñón, S. Hughes, and S. R. Weiss. "Characterization of the Leader Papain-Like Protease of MHV-A59." In Advances in Experimental Medicine and Biology. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1899-0_68.

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