Changes in bacteriophage T7 virion structure at the initiation of infection.
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abstract
Five proteins are ejected from the bacteriophage T7 virion at the initiation of infection. The three known proteins of the internal core enter the infected cell; all three must both disaggregate from their structure in the mature virion and also almost completely unfold in order to leave the head and pass through the head-tail connector. Two small proteins, the products of genes 6.7 and 7.3, also are ejected from the infecting virion. Gp6.7 and gp7.3 were not previously described as structural virion components, leading to a re-appraisal of the stoichiometry of virion proteins. Gp6.7 is found in tail-less particles and is defined as a head protein, whereas gp7.3 is localized in the tail. Gene 6.7 may be important in morphogenesis; mutants defective in this late gene yield a reduced burst of progeny. Gene 7.3 is essential for virion assembly but, although normally present, its product gp7.3 is not required in a mature particle. Particles assembled in the absence of gp7.3 contain tail fibers but fail to adsorb to cells.
