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Journal of Virology, September 2004, p. 9790-9797, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.9790-9797.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Integral Membrane Protein P16 of Bacteriophage PRD1 Stabilizes the Adsorption Vertex Structure

Silja T. Jaatinen, Salla J. Viitanen, Dennis H. Bamford, and Jaana K. H. Bamford*

Faculty of Biosciences and Institute of Biotechnology, Viikki Biocenter, University of Helsinki, Helsinki, Finland

Received 13 February 2004/ Accepted 26 April 2004

The icosahedral membrane-containing double-stranded DNA bacteriophage PRD1 has a labile receptor binding spike complex at the vertices. This complex, which is analogous to that of adenovirus, is formed of the penton protein P31, the spike protein P5, and the receptor binding protein P2. Upon infection, the internal phage membrane transforms into a tubular structure that protrudes through a vertex and penetrates the cell envelope for DNA injection. We describe here a new class of PRD1 mutants lacking virion-associated integral membrane protein P16. P16 links the spike complex to the viral membrane and is necessary for spike stability. We also show that the unique vertex used for DNA packaging is intact in the P16-deficient particle, indicating that the 11 adsorption vertices and the 1 portal vertex are functionally and structurally distinct.

* Corresponding author. Mailing address: Viikki Biocenter 2, P.O. Box 56 (Viikinkaari 5), FIN-00014 University of Helsinki, Finland. Phone: 358-9-19159101. Fax: 358-9-19159098. E-mail: jaana.bamford{at}helsinki.fi.

Journal of Virology, September 2004, p. 9790-9797, Vol. 78, No. 18
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.18.9790-9797.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Karhu, N. J., Ziedaite, G., Bamford, D. H., Bamford, J. K. H. (2007). Efficient DNA Packaging of Bacteriophage PRD1 Requires the Unique Vertex Protein P6. J. Virol. 81: 2970-2979 [Abstract] [Full Text]  


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