Abstract
Vaccinia virus has a complex structure. Thin sections of virus particles show three structural components: the outer envelope, the lateral bodies and a central structure, known as the core, which contains the virus DNA (Dales, 1963). Easterbrook (1966) showed that treatment with the nonionic detergent NP40, in the presence of 2-mercaptoethanol (2 ME) leads to the dissociation of the outer membrane and release of the core.
By polyacrylamide gel electrophoresis, Holowczak & Joklik (1967) identified at least 17 structural polypeptides, three of which were associated with the core. Katz & Moss (1970) showed that some of these polypeptide peaks could be further separated into two to three polypeptides, thus increasing the total number of resolved structural polypeptides to 22.
Our knowledge concerning the arrangement of vaccinia virus polypeptides on the particle surface is very limited. The present paper attempts to determine which of the virus polypeptides is situated on the surface.