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Journal of Virology, May 2002, p. 4866-4872, Vol. 76, No. 10
0022-538X/02/$04.00+0 DOI: 10.1128/JVI.76.10.4866-4872.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
ius,1,2 and Dennis H. Bamford1*
Department of Biosciences and Institute of Biotechnology, University of Helsinki, Helsinki, Finland,1 Department of Biochemistry and Biophysics, Vilnius University, Vilnius, Lithuania2
Received 15 November 2001/ Accepted 15 February 2002
The lipid-containing bacteriophage PRD1 infects a variety of gram-negative cells by injecting its linear double-stranded DNA genome into the host cell cytoplasm, while the protein capsid is left outside. The virus membrane and several structural proteins are involved in phage DNA entry. In this work we identified a new infectivity protein of PRD1. Disruption of gene XXXII resulted in a mutant phenotype defective in phage reproduction. The absence of the protein P32 did not compromise the particle assembly but led to a defect in phage DNA injection. In P32-deficient particles the phage membrane is unable to undergo a structural transformation from a spherical to a tubular form. Since P32- particles are able to increase the permeability of the host cell envelope to a degree comparable to that found with wild-type particles, we suggest that the tail-tube formation is needed to eject the DNA from the phage particle rather than to reach the host cell interior.
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