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  • American Society for Microbiology  (3)
  • 1980-1984  (3)
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  • American Society for Microbiology  (3)
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  • 1980-1984  (3)
Year
  • 1
    Online Resource
    Online Resource
    Identification of B-lymphotropic papovavirus-coded proteins
    American Society for Microbiology ; 1983
    In:  Journal of Virology Vol. 45, No. 2 ( 1983-02), p. 872-875
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 45, No. 2 ( 1983-02), p. 872-875
    Abstract: The lymphotropic papovavirus (LPV)-specific mRNAs were translated in vitro in rabbit reticulocyte lysates. The specific products were 84,000-dalton (84K), 41K, 35K, and 26K proteins. Immunoprecipitation with anti-LPV hamster sera and analysis of partially purified LPV virions showed that the last three proteins were the LPV capsid proteins, and we designated the 41K, 35K, and 26K proteins VP1 (major capsid protein), VP2, and VP3, respectively. Several characteristics, such as the small amount of mRNA for the 84K protein at late stages of infection, its absence from partially purified virus preparations, no common tryptic peptides between the 84K and 41K proteins, and the pattern of in vivo phosphorylation, suggest that the 84K protein is not a simple dimer of the 41K protein. Normal human sera and sera from certain leukemic patients positive for antibody to LPV viral antigens immunoprecipitated the 41K protein.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.45.2.872-875.1983
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1983
    detail.hit.zdb_id: 1495529-5
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  • 2
    Online Resource
    Online Resource
    Characterization of N-type and dually permissive cells segregated from mouse fibroblasts whose Fv-1 phenotype could be modified by another independently segregating gene(s)
    American Society for Microbiology ; 1982
    In:  Journal of Virology Vol. 41, No. 1 ( 1982-01), p. 145-152
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 41, No. 1 ( 1982-01), p. 145-152
    Abstract: Though the inbred DDD mouse strain is essentially of the N type, the primary culture of this strain was about 100-fold more sensitive to B-tropic WN1802B virus than were the typical N-type strains (C3H/He, C57L, etc.). After cloning, DDD mouse cells segregated two types of cells, typical N-type cells and cells lacking in Fv-1 restriction. As both types of cells so far tested retained glucose-6-phosphatase-1 coded by a locus closely linked to Fv-1 and genetic cross experiments indicated the presence of a gene(s) modifying the Fv-1 phenotype, variation in Fv-1 restriction could presumably be brought about by genetic changes in a gene(s) other than Fv-1 itself. N-type and dually permissive cell clones were similarly established from the inbred G mouse. Compositions of polypeptides labeled with [35S]methionine in the N-type and dually permissive cells of DDD and G mouse origins were compared by two-dimensional gel electrophoresis. The polypeptide maps of these cells were similar except for a few spots. Among these dissimilar spots, a spot of about 20,000 daltons with a pI of about 5.5 was always present in N-type cells, whereas it was absent in dually permissive cells. In DDD mouse-derived clones, a proportional relation was observed between the intensity of the spot and the restriction to the B-tropic virus.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.41.1.145-152.1982
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1982
    detail.hit.zdb_id: 1495529-5
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  • 3
    Online Resource
    Online Resource
    Antibodies against a nonapeptide of polyomavirus middle T antigen: cross-reaction with a cellular protein(s)
    American Society for Microbiology ; 1983
    In:  Journal of Virology Vol. 48, No. 3 ( 1983-12), p. 709-720
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 48, No. 3 ( 1983-12), p. 709-720
    Abstract: Antibodies were raised against the sequence Glu-Glu-Glu-Glu-Tyr-Met-Pro-Met -Glu, which represents a part of the middle T antigen of polyomavirus that is considered to be important in inducing the phenotype of transformed cells. The antibodies reacted with native as well as denatured middle T antigens. In addition, the antibodies immunoprecipitated a cellular protein with an apparent molecular weight of 130,000 (130K) from mouse and rat cells. In some cases, a 33K protein was also immunoprecipitated. Immunoprecipitation of middle T antigen as well as 130K and 33K proteins was blocked by the peptide. The antibodies labeled microfilaments of untransformed mouse, rat, human, and chicken cells by immunofluorescence. This labeling was also blocked by the peptide. The labeling pattern and distribution under a variety of conditions were indistinguishable from those of anti-actin antibodies, although no evidence has been obtained to indicate that the anti-peptide antibodies react with actin. The 130K protein migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis slightly slower than chicken gizzard vinculin (130K) and slightly faster than myosin light-chain kinase of chicken smooth muscle (130K). Neither of these proteins absorbed the anti-peptide antibodies. The 33K protein does not seem to be tropomyosin (32K to 40K).
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/jvi.48.3.709-720.1983
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1983
    detail.hit.zdb_id: 1495529-5
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