1887

Abstract

Summary

SDS-Page of the 190 virus of , using a discontinuous buffer system, revealed two major capsid polypeptides of mol. wt. 88K and 83K (p88 and p83) and a minor polypeptide, p78. Peptide mapping by both limited proteolysis and selective chemical cleavage showed p83 and p78 to be closely related to p88. The origin of p83/p78 could not be explained by proteolysis of p88 during virus preparation and storage. In rabbit reticulocyte lysates, denatured dsRNA directed the synthesis of a single major translation product which was identical to capsid polypeptide p88 on the basis of coelectrophoresis, immunoprecipitation and peptide mapping. No translation products comparable in size to p83 or p78 were detected . These data indicated that the capsid of the 190 virus is encoded by a single gene and verified the classification of the virus as a member of the family . Radioiodination of intact virus under conditions considered optimum for surface-specific iodination showed p88 to be more readily available for labelling than p83 or p78. Furthermore, when Western blots of capsid polypeptides were reacted with an antiserum to glutaraldehyde-stabilized virus (190-G), p88 was more reactive to 190-G antibodies than was p83/p78. These results suggest p88 is external to p83/p78 in the capsid.

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/content/journal/jgv/10.1099/0022-1317-68-7-1791
1987-07-01
2019-10-21
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-68-7-1791
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