Mouse Hepatitis Virus Gene 5b Protein Is a New Virion Envelope Protein

Yu, Xuekui; Bi, Weizhen; Weiss, Susan R.; Leibowitz, Julian L.

doi:10.1006/viro.1994.1430

Cited by 117 publications

(138 citation statements)

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“…Immunoprecipitation was performed as described previously (Yu et al, 1994). When monoclonal antibodies were used for immunoprecipitation, Protein A beads were precoated with goat anti-mouse IgG.…”

Section: Plasmids and Transfectionsmentioning

confidence: 99%

Localization of mouse hepatitis virus open reading frame 1A derived proteins

Bi¹,

Piñón²,

Hughes³

et al. 1998

J Neurovirol

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We have investigated the intracellular localization of proteolytic cleavage products encoded in the 5' portion of mouse hepatitis virus (MHV) gene 1. Immuno¯uorescent labeling of cells with an antiserum which recognizes p28, the ORF1a N-terminal cleavage product, resulted in widespread somewhat granular cytoplasmic staining, indicating that this protein is widely distributed in the cytoplasm of MHV-infected, but not control uninfected cells. Immunouorescent staining of infected cells with antisera which recognize the downstream polypeptides, p65, p240 and p290 labeled discrete vesicular perinuclear structures. Double immuno¯uorescent labeling of BHK cells expressing the MHV receptor (BHK MHVR1 ) and infected with MHV-A59 with a Golgi-speci®c anti-mannosidase II monoclonal antibody and with antiserum recognizing each of these anti-MHV ORF1a polypeptides, showed that the p240 and p290 polypeptides were localized in discrete vesicular structures that overlapped the Golgi complex. Labeling with antibodies speci®c for p65 colocalized with the Golgi region, and showed staining of the perinuclear cytoplasm as well. Plasmids containing sequences contained in the ®rst 6.75 kb of ORF1a have been expressed using the coupled vaccinia virus-T7 polymerase system. Immuno¯uorescent labeling of transfectants with the anti-ORF1a antisera showed patterns of antigen distribution similar to those observed in cells infected with MHV-A59. A deletion analysis with constructs containing only portions of the ORF1a sequence indicated that 303 amino acids containing the ®rst papain-like protease domain (PLP-1) was suf®cient to associate this protein with the Golgi.

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Section: Plasmids and Transfectionsmentioning

confidence: 99%

Localization of mouse hepatitis virus open reading frame 1A derived proteins

Bi¹,

Piñón²,

Hughes³

et al. 1998

J Neurovirol

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“…The small membrane protein (E)has only recently been discovered and may playa role in either uncoating or assembly of the virus (Yu et al 1994).It makes up only a small part of the viral envelope and is believed to have catalytic functions. Some MHV strains, like other Group 2 coronaviruses (BCV, HCV-OC43, HEV, TCV), possess a fourth glycosylated envelope protein, the haemagglutinin/esterase (HE) (King et al 1985.…”

Section: Virus Structurementioning

confidence: 99%

Enterotropic mouse hepatitis virus

Homberger

1997

Lab Anim

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SummaryMouse hepatitis virus (MHVI, the coronavirus of the mouse, is the most common viral pathogen in contemporary laboratory mouse colonies throughout the world. It is highly contagious with variable clinical manifestations. The majority of infections are subclinical, but can still significantly influence biological responses, thus interfering with research, mainly in the field of immunology. MHV has been intensively studied from a number of research perspectives and has become the prototype for studying the molecular biology of coronaviruses. MHV contains a single-stranded} positive-sense RNA genome ranging from 27 to 31 kb}which is divided into seven genes. Virions consist of four to five structural proteins. There are many MHV strains that vary in virulence, organotropism and cell tropism} and are constantly evolving by naturally occurring mutation and recombination. Based on pathogenesis studies MHV strains are usually grouped according to their primary tissue tropism into two biotypes: polytropic and enterotropic. Enterotropic strains of MHV replicate in the intestinal mucosa and only rarely spread to other tissues. No morphological structure of the virion has as yet been identified that is responsible for enterotropism. The course of an MHV infection is dependent on the virus strain and host factors. Generally, MHV causes an acute, self-limiting infection which is inapparent in adult mice. Neonates are highly susceptible to disease and show high mortality. In an enzootically infected colony, however, they are protected by maternally derived passive immunity. Detection of MHV infections depends on serological screening of colonies. MHV is controlled by culling and rederivation of the affected colony using hysterectomy or embryo transfer or by elimination through cessation of breeding.

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“…It spans the membrane bilayer three times, having a short aminoterminal domain on the exterior of the virus and a large carboxy terminus, containing more than half the mass of the molecule, in the virion interior (48). By contrast, E is a minor structural protein, in both size and stoichiometry, and was only relatively recently identified as a constituent of viral particles (17,33,62). The most prominent virion protein, S, makes a single pass through the membrane envelope, with almost the entire molecule forming an amino-terminal ectodomain.…”

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confidence: 99%

Retargeting of Coronavirus by Substitution of the Spike Glycoprotein Ectodomain: Crossing the Host Cell Species Barrier

Kuo

Godeke

Raamsman

et al. 2000

J Virol

333

525

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Coronaviruses generally have a narrow host range, infecting one or just a few species. Using targeted RNA recombination, we constructed a mutant of the coronavirus mouse hepatitis virus (MHV) in which the ectodomain of the spike glycoprotein (S) was replaced with the highly divergent ectodomain of the S protein of feline infectious peritonitis virus. The resulting chimeric virus, designated fMHV, acquired the ability to infect feline cells and simultaneously lost the ability to infect murine cells in tissue culture. This reciprocal switch of species specificity strongly supports the notion that coronavirus host cell range is determined primarily at the level of interactions between the S protein and the virus receptor. The isolation of fMHV allowed the localization of the region responsible for S protein incorporation into virions to the carboxyterminal 64 of the 1,324 residues of this protein. This establishes a basis for further definition of elements involved in virion assembly. In addition, fMHV is potentially the ideal recipient virus for carrying out reverse genetics of MHV by targeted RNA recombination, since it presents the possibility of selecting recombinants, no matter how defective, that have regained the ability to replicate in murine cells.The family Coronaviridae contains the causative agents of a number of significant respiratory and enteric diseases affecting humans, other mammals, and birds (55). One of the hallmarks of this family is that most of its members exhibit a very strong degree of host species specificity, the molecular basis of which is thought to reside in the particularity of the interactions of individual viruses with their corresponding host cell receptors.Coronaviruses have positive-stranded RNA genomes, on the order of 30 kb in length, that are packaged by a nucleocapsid protein (N) into helical ribonucleoprotein structures (31). The nucleocapsid is incorporated into viral particles by budding through the membrane of the intermediate compartment between the endoplasmic reticulum and the Golgi complex (26, 57). Subsequent to budding, it may acquire a spherical, possibly icosahedral superstructure (43,44). The virion envelope surrounding the nucleocapsid contains a minimal set of three structural proteins: the membrane glycoprotein (M), the small envelope protein (E), and the spike glycoprotein (S). In some coronaviruses, other proteins may also be present; these include a hemagglutinin-esterase (HE) (34, 54) and the product of the internal open reading frame of the N gene (I protein) (12, 53), neither of which is essential for virus infectivity.M is the most abundant of the virion structural proteins. It spans the membrane bilayer three times, having a short aminoterminal domain on the exterior of the virus and a large carboxy terminus, containing more than half the mass of the molecule, in the virion interior (48). By contrast, E is a minor structural protein, in both size and stoichiometry, and was only relatively recently identified as a constituent of viral particles (17,33,...

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Mouse Hepatitis Virus Gene 5b Protein Is a New Virion Envelope Protein

Cited by 117 publications

References 0 publications

Localization of mouse hepatitis virus open reading frame 1A derived proteins

Localization of mouse hepatitis virus open reading frame 1A derived proteins

Enterotropic mouse hepatitis virus

Retargeting of Coronavirus by Substitution of the Spike Glycoprotein Ectodomain: Crossing the Host Cell Species Barrier

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