DNA-Protein Interactions and Protein-Protein Interactions in Filamentous Bacteriophage Assembly

Implications for Epitope Display
  • Richard N. Perham
  • Donald A. Marvin
  • Martyn F. Symmons
  • Liam C. Welsh
  • Tamsin D. Terry

Abstract

The virion of the filamentous bacteriophage fd (fl and M13 are very similar strains) is a flexible rod about 1 μm long and 6 nm in diameter, comprising a tubular sheath of approx. 2700 copies of the major coat protein subunit surrounding a DNA core. The DNA is a single-stranded circular molecule of 6408 nucleotides embodying 10 genes; these genes are tightly packed and, in some instances, overlapping, apart from a short region (the intergenic space) which encodes no protein component but which contains a double-stranded helical hairpin loop responsible for initiating assembly of the virion. There are a few copies (about 5) of each of two minor coat proteins at the two ends of the virion: gVIIp and gIXp at the end where assembly is initiated, and glllp and gVIp at the end where the process is terminated [for general reviews, see Model & Russe1,1988; Russel, 1991)].

Keywords

Coat Protein Filamentous Bacteriophage Negative Charge Density Positive Charge Density Foreign Peptide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Richard N. Perham
    • 1
  • Donald A. Marvin
    • 1
  • Martyn F. Symmons
    • 1
  • Liam C. Welsh
    • 1
  • Tamsin D. Terry
    • 1
  1. 1.Cambridge Centre for Molecular Recognition Department of BiochemistryUniversity of CambridgeCambridgeEngland

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