Sialylatin of glycoproteins of murine mammary tumor virus, murine leukemia virus, and Mason-Pfizer monkey virus.
Neuraminidase treatment of mouse mammary tumor virus, Rauscher murine leukemia virus, and Mason-Pfizer monkey virus resulted in loss of their capacity to inhibit hemagglutination of influenza virus. Hemagglutination-inhibition activity of these RNA tumor viruses could be restored by in vitro resialylation catalyzed by sialyl transferase. The major glycoprotein in the intact envelope of desialylated and, to some extent, native virions could be specificallly labeled in vitro with CMP-(14C) sialic acid. These studies further characterize the individual glycoproteins of mouse mammary tumor virus, Rauscher murine leukemia virus, and Mason-Pfizer monkey virus.
D000818:Animals; D002474:Cell-Free System; D006023:Glycoproteins / Q000096:biosynthesis*; D000882:Haplorhini; D006387:Hemagglutination, Viral / Q000187:drug effects; D008324:Mammary Tumor Virus, Mouse / Q000187:drug effects / Q000378:metabolism*; D009439:Neuraminidase / Q000494:pharmacology; D009858:Oncogenic Viruses / Q000187:drug effects / Q000378:metabolism*; D011925:Rauscher Virus / Q000187:drug effects / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism*; D012799:Sialyltransferases / Q000378:metabolism; D014764:Viral Proteins / Q000096:biosynthesis*
D006023:Glycoproteins; D012794:Sialic Acids; D014764:Viral Proteins; D012799:Sialyltransferases; D009439:Neuraminidase