The Tailless Icosahedral Membrane Virus PRD1 Localizes the Proteins Involved in Genome Packaging and Injection at a Unique Vertex
Open Access
- 15 July 2003
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 77 (14) , 7863-7871
- https://doi.org/10.1128/jvi.77.14.7863-7871.2003
Abstract
The double-stranded DNA (dsDNA) virus PRD1 carries its genome in a membrane surrounded by an icosahedral protein shell. The shell contains 240 copies of the trimeric P3 protein arranged with a pseudo T = 25 triangulation that is reminiscent of the mammalian adenovirus. DNA packaging and infection are believed to occur through the vertices of the particle. We have used immunolabeling to define the distribution of proteins on the virion surface. Antibodies to protein P3 labeled the entire surface of the virus. Most of the 12 vertices labeled with antibodies directed against proteins P5, P2, and P31. These proteins are known to function in virus binding to the cell surface. Proteins P6, P11, and P20 were found on a single vertex per virion. The P6 and P20 proteins are believed to function in DNA packaging. Protein P11 is a pilot protein that is involved in a complex that mediates the early stages of DNA entry to the host cell. Labeling with antibodies to P5 or P2 did not affect the labeling of P6, the unique vertex protein. Labeling with antibodies to the unique vertex protein P6 interfered with the labeling by antibodies to the unique vertex protein P20. We conclude that PRD1 utilizes 11 of its vertices for initial receptor binding. It utilizes a single, unique vertex for both DNA packing during assembly and DNA delivery during infection.Keywords
This publication has 78 references indexed in Scilit:
- Minor proteins, mobile arms and membrane–capsid interactions in the bacteriophage PRD1 capsidNature Structural & Molecular Biology, 2002
- The Lytic Enzyme of Bacteriophage PRD1 Is Associated with the Viral MembraneJournal of Bacteriology, 2002
- Combined EM/X-Ray Imaging Yields a Quasi-Atomic Model of the Adenovirus-Related Bacteriophage PRD1 and Shows Key Capsid and Membrane InteractionsStructure, 2001
- A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage φ6Journal of Molecular Biology, 1999
- Bacteriophage PRD1 contains a labile receptor-binding structure at each vertex 1 1Edited by A. KlugJournal of Molecular Biology, 1999
- Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage φ6Journal of Molecular Biology, 1998
- The core of the mammalian centriole contains γ-tubulinCurrent Biology, 1995
- The Refined Crystal Structure of Hexon, the Major Coat Protein of Adenovirus Type 2, at 2·9 Å ResolutionJournal of Molecular Biology, 1994
- Crystallization of the Major Coat Protein of PRD1, a Bacteriophage with an Internal MembraneJournal of Molecular Biology, 1993
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976