Synthesis and subcellular localization of the murine coronavirus nucleocapsid protein.
The synthesis and processing of the nucleocapsid protein (pp60) of the JHM strain of murine coronaviruses were examined. Pulse-chase experiments showed that pp60 was synthesized initially as a protein of approximately 57,000 in molecular weight (p57). Immunoprecipitation using mouse anti-JHMV antiserum indicated that p57 was virus specific. Immunoprecipitation with monoclonal antibodies specific for pp60 showed that p57 was antigenically related to pp60 and was not phosphorylated, while the intracellular protein that comigrated with the virion nucleocapsid protein, pp60, was phosphorylated. The p57 was found exclusively in the cytosol while the majority of pp60 was associated with the membrane fraction but pp60 was not an integral membrane protein.
D000818:Animals; D002213:Capsid / Q000032:analysis / Q000276:immunology / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis*; D003600:Cytosol / Q000032:analysis*; D000939:Epitopes / Q000032:analysis; D051379:Mice; D008970:Molecular Weight; D006517:Murine hepatitis virus / Q000378:metabolism*; D010766:Phosphorylation; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D000939:Epitopes; D011498:Protein Precursors