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 × 10, based on polyacrylamide gel electrophoresis experiments in the presence of formaldehyde. The virus contains one major polypeptide, mol. wt. 70 × 10 as determined by polyacrylamide gel electrophoresis and by chromatography on Sepharose 6B in the presence of 6 -guanidine. Further evidence for the presence of a single major polypeptide was obtained by tryptic peptide analysis of S-methionine labelled virus. The mol. wt. of a protein oligomer produced by adjusting the pH of virus suspensions to 3.5 was 200 × 10. 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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