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The structure of vesicular exanthema virus, the prototype member of the calicivirus group, has been studied in more detail. The RNA comprises 18% of the virus particle and has a mol. wt. of about 2.8 × 106, based on polyacrylamide gel electrophoresis experiments in the presence of formaldehyde. The virus contains one major polypeptide, mol. wt. 70 × 103 as determined by polyacrylamide gel electrophoresis and by chromatography on Sepharose 6B in the presence of 6 m-guanidine. Further evidence for the presence of a single major polypeptide was obtained by tryptic peptide analysis of 35S-methionine labelled virus. The mol. wt. of a protein oligomer produced by adjusting the pH of virus suspensions to 3.5 was c. 200 × 103. On the basis of these data we propose a T = 3 model for the virus capsid incorporating 180 copies of the virus protein.
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