Protrusions covering the surface of intracellular mature virions (IMV), termed by us surface tubular elements (STE), are released in a quasi-intact form during stripping of the envelope. The concentrated, reproducibly isolable STE were shown to contain the 58-kDa 4c polypeptide and prominent protein antigens residing at the surface of IMV. The major core protein 4b, identified as a minor contaminant of STE, presumably became detached along with STE during the shearing off process. Antibodies against protein 4b became specifically bound to the surface of isolated cores, where a palisade layer of rodlets occurs. The same antibodies absorbed onto isolated STE where similar rodlets were evident. Based on the new observations we constructed a model of the organization of the IMV envelope and its relationship to the core.
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