Abstract
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.
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Keywords
- Rough Endoplasmic Reticulum
- Viral Glycoprotein
- Mouse Hepatitis Virus
- Structural Poly
- Intracellular Synthesis
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References
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© 1981 Springer Science+Business Media New York
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Holmes, K.V., Doller, E.W., Behnke, J.N. (1981). Analysis of the Functions of Coronavirus Glycoproteins by Differential Inhibition of Synthesis with Tunicamycin. In: ter Meulen, V., Siddell, S., Wege, H. (eds) Biochemistry and Biology of Coronaviruses. Advances in Experimental Medicine and Biology, vol 142. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0456-3_11
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DOI: https://doi.org/10.1007/978-1-4757-0456-3_11
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