Analysis of the Functions of Coronavirus Glycoproteins by Differential Inhibition of Synthesis with Tunicamycin
The virion associated polypeptides of the A59 strain of mouse hepatitis virus (MHV) have been studied extensively (Sturman, 1977; Sturman and Holmes, 1977; Sturman et al., 1980) and are described by Dr. Sturman in this symposium. The nucleocapsid polypeptide N is phosphorylated and has a molecular weight of 50K. Two glycoproteins are associated with the viral envelope. The peplomers are composed of the glycoprotein E2(MW ≃ 180K) which may be proteolytically cleaved to yield two molecules which both migrate with an apparent molecular weight of 90K. The glycoprotein El (MW ≃ 23K) is deeply embedded in the viral membrane with the small glycosolated portion protruding. We have studied the intracellular synthesis of these structural polypeptides of A59 in the 17 clone 1 line (17 C1 1) of spontaneously transformed BALB/c 3T3 cells. A59 acts as a moderate virus in 17 C1 1 cells causing limited cell fusion. Virus particles are shed from intact cells following a 6 to 7 hour latent period at 37°, and the yield of infectious virus at 24 hours is 108 to 109 PFU/ml.
KeywordsRough Endoplasmic Reticulum Viral Glycoprotein Mouse Hepatitis Virus Structural Poly Intracellular Synthesis
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