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  • American Society for Microbiology  (6)
  • 1990-1994  (6)
Material
Publisher
  • American Society for Microbiology  (6)
Person/Organisation
Language
Years
  • 1990-1994  (6)
Year
  • 1
    Online Resource
    Online Resource
    A second envelope glycoprotein mediates neutralization of a pestivirus, hog cholera virus
    American Society for Microbiology ; 1992
    In:  Journal of Virology Vol. 66, No. 6 ( 1992-06), p. 3677-3682
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 66, No. 6 ( 1992-06), p. 3677-3682
    Abstract: Several monoclonal antibodies (MAbs) raised against hog cholera virus (HCV) reacted with the HCV structural glycoprotein gp44/48 and neutralized the virus. The presence of HCV gp44/48 on the viral surface was directly demonstrated by immunogold electron microscopy. Eight anti-HCV gp44/48 MAbs were tested by immunoperoxidase assay against a panel of pestivirus strains. Each MAb showed a distinct pattern of reactivity with HCV strains. It is suggested that the MAbs are well suited for epidemiological investigations of HCV outbreaks.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.66.6.3677-3682.1992
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1495529-5
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Constitutive production of alpha and beta interferons in mutant human cell lines
    American Society for Microbiology ; 1994
    In:  Journal of Virology Vol. 68, No. 6 ( 1994-06), p. 4057-4062
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 68, No. 6 ( 1994-06), p. 4057-4062
    Abstract: Alpha and beta interferons control expression of a selectable marker in the human hypoxanthine phosphoribosyltransferase-negative cell line 2fTGH, in which transcription of gpt is regulated by the upstream region of an interferon-responsive human gene. Selection of mutagenized 2fTGH cells in hypoxanthine-aminopterin-thymidine medium yielded mutants in one recessive (C1) and two dominant (C2 and C3) complementation groups. The mutants constitutively expressed low levels of beta interferon (C1), alpha interferon (C2), or both (C3).
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.68.6.4057-4062.1994
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1994
    detail.hit.zdb_id: 1495529-5
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  • 3
    Online Resource
    Online Resource
    Hog cholera virus: molecular composition of virions from a pestivirus
    American Society for Microbiology ; 1991
    In:  Journal of Virology Vol. 65, No. 9 ( 1991-09), p. 4705-4712
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 65, No. 9 ( 1991-09), p. 4705-4712
    Abstract: Virions from hog cholera virus (HCV), a member of the genus Pestivirus, were analyzed by using specific antibodies. The nucleocapsid protein was found to be a 14-kDa molecule (HCV p14). An equivalent protein could also be demonstrated for virions from another pestivirus, bovine viral diarrhea virus. The HCV envelope is composed of three glycoproteins, HCV gp44/48, gp33, and gp55. All three exist in the form of disulfide-linked dimers in virus-infected cells and in virions; HCV gp44/48 and gp55 each form homodimers, whereas gp55 is also found dimerized with gp33. Such complex covalent interactions between structural glycoproteins have not been described so far for any RNA virus.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.65.9.4705-4712.1991
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1495529-5
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  • 4
    Online Resource
    Online Resource
    Structural proteins of hog cholera virus expressed by vaccinia virus: further characterization and induction of protective immunity
    American Society for Microbiology ; 1991
    In:  Journal of Virology Vol. 65, No. 2 ( 1991-02), p. 589-597
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 65, No. 2 ( 1991-02), p. 589-597
    Abstract: A cDNA fragment covering the genomic region that encodes the structural proteins of hog cholera virus (HCV) was inserted into the tk gene of vaccinia virus. Expression studies with vaccinia virus/HCV recombinants led to identification of HCV-specific proteins. The putative HCV core protein p23 was demonstrated for the first time by using an antiserum against a bacterial fusion protein. The glycoproteins expressed by vaccinia virus/HCV recombinant migrated on sodium dodecyl sulfate-gels identically to glycoproteins precipitated from HCV-infected cells. A disulfide-linked heterodimer between gp55 and gp33 previously detected in HCV-infected cells was also demonstrated after infection with the recombinant virus. The vaccinia virus system allowed us to identify, in addition to the heterodimer, a disulfide-linked homodimer of HCV gp55. The vaccinia virus/HCV recombinant that expressed all four structural proteins induced virus-neutralizing antibodies in mice and swine. After immunization of pigs with this recombinant virus, full protection against a lethal challenge with HCV was achieved. A construct that lacked most of the HCV gp55 gene failed to induce neutralizing antibodies but induced protective immunity.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.65.2.589-597.1991
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1495529-5
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  • 5
    Online Resource
    Online Resource
    Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer
    American Society for Microbiology ; 1990
    In:  Journal of Virology Vol. 64, No. 8 ( 1990-08), p. 3563-3569
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 64, No. 8 ( 1990-08), p. 3563-3569
    Abstract: Neutralizing monoclonal antibodies directed against hog cholera virus (HCV) precipitated two HCV-encoded glycoproteins, HCV gp55 and HCV gp33. Immunoassay with bacterial fusion proteins and Western immunoblotting with extracts from infected cells revealed that the antibodies recognized only HCV gp55. Coprecipitation of HCV gp33 was shown to be due to intermolecular disulfide bridges. One of the antibodies also reacted with the major glycoprotein of another pestivirus, bovine viral diarrhea virus (BVDV). The analogous BVDV glycoproteins exhibited a distribution of cysteine residues which was almost identical to that of HCV gp55 and gp33. The two BVDV glycoproteins were also linked by disulfide bridges.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.64.8.3563-3569.1990
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1990
    detail.hit.zdb_id: 1495529-5
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  • 6
    Online Resource
    Online Resource
    Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus
    American Society for Microbiology ; 1993
    In:  Journal of Virology Vol. 67, No. 12 ( 1993-12), p. 7088-7095
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 67, No. 12 ( 1993-12), p. 7088-7095
    Abstract: The polyprotein of classical swine fever virus starts with the nonstructural protein p23, which is followed by the nucleocapsid protein p14. Proteolytic cleavage between p23 and p14 was demonstrated in a cell-free transcription-translation system. Successive truncation of the cDNA used for the transcription indicated that the proteolytic activity responsible for the cleavage between p23 and p14 resides within p23. In order to determine the cleavage site between these two proteins, the respective genomic regions were expressed in two different expression systems. N-terminal sequencing of the resulting p14-related proteins revealed that cleavage occurs between Cys-168 and Ser-169. Comparison of the sequence around the cleavage site with sequences of other pestiviruses suggests a conserved processing site between similar proteins.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.67.12.7088-7095.1993
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 1495529-5
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