Biomedical subjects

P Dreiding

Publications and source records attributed to P Dreiding.

3 recordsLinked to original sources

PubMed1985

Polyclonal and monoclonal antibodies to the interferon-inducible protein Mx of influenza virus-resistant mice.

Interferon-alpha/beta induces in cells from mice carrying the influenza virus resistance allele Mx+ the synthesis of a unique 75,000-dalton protein (designated here protein Mx) that was not detectable in interferon-treated cells from Mx- mice lacking the resistance allele (Horisberger, M. A., Staeheli, P., and Haller, O. (1983) Proc. Natl. Acad. Sci. U. S. A. 80, 1910-1914). We have immunized Mx- BALB/c mice with extracts of interferon-treated cells from congenic Mx+ BALB X A2G-Mx mice. Resulting hyperimmune sera immunoprecipitated a single interferon-inducible 75,000-dalton protein of Mx+ embryo cells. Sera did not react with any interferon-inducible protein of Mx- cells. Synthesis of the immunoprecipitable 75,000-dalton protein Mx was induced by interferon-alpha/beta but not by interferon-gamma in Mx+ cells of diverse genetic backgrounds. Monoclonal antibodies to protein Mx were selected in similar immunoprecipitation assays. One discrete in vitro translation product of relevant mRNA reacted with polyclonal and monoclonal antibodies and was indistinguishable from in vivo synthesized protein Mx.

Animals↗

PubMed1985

Interferon-induced protein Mx accumulates in nuclei of mouse cells expressing resistance to influenza viruses.

In mouse cells carrying the dominant influenza resistance allele Mx+ (but not in Mx- cells) interferon-alpha/beta (IFN) induces an efficient antiviral state against influenza viruses and, concomitantly, the synthesis of a 75,000-Da protein (protein Mx). Here, indirect immunofluorescence using monoclonal antibodies was used to demonstrate that protein Mx accumulates in the nucleus of IFN-treated Mx+ cells, suggesting a nuclear site of action. Protein Mx is present in the nucleus of untreated influenza virus-resistant macrophages freshly explanted from the peritoneal cavity of Mx+ mice but is lost with time in culture when peritoneal macrophages become permissive for influenza virus.

Alleles↗

PubMed1984

Various human interferon alpha subclasses cross-react with common receptors: their binding affinities correlate with their specific biological activities.

Seven different human interferon (IFN) alpha subtypes were compared with regard to competitive inhibition of specific high-affinity binding of 125I-labeled IFN alpha-2 to human and bovine cells. All IFNs tested (alpha-1, -2, -4, -5, -6, -7, -8) competed for common binding sites. Marked differences in the binding affinities were observed between IFN alpha-1 and IFN alpha-2. The binding affinities of the various subtypes correlated with the respective specific biological activities determined in an antiviral assay. These observations suggest that at least some biological effects of IFNs are initiated by receptor activation and depend quantitatively on the degree of receptor saturation.

Animals↗