The Unique Vertex of Bacterial Virus PRD1 Is Connected to the Viral Internal Membrane
AUTOR(ES)
Strömsten, Nelli J.
FONTE
American Society for Microbiology
RESUMO
Icosahedral double-stranded DNA (dsDNA) bacterial viruses are known to package their genomes into preformed procapsids via a unique portal vertex. Bacteriophage PRD1 differs from the more commonly known icosahedral dsDNA phages in that it contains an internal lipid membrane. The packaging of PRD1 is known to proceed via preformed empty capsids. Now, a unique vertex has been shown to exist in PRD1. We show in this study that this unique vertex extends to the virus internal membrane via two integral membrane proteins, P20 and P22. These small membrane proteins are necessary for the binding of the putative packaging ATPase P9, via another capsid protein, P6, to the virus particle.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=155016Documentos Relacionados
- The Tailless Icosahedral Membrane Virus PRD1 Localizes the Proteins Involved in Genome Packaging and Injection at a Unique Vertex
- The Lytic Enzyme of Bacteriophage PRD1 Is Associated with the Viral Membrane
- The Lytic Enzyme of Bacteriophage PRD1 Is Associated with the Viral Membrane
- Integral Membrane Protein P16 of Bacteriophage PRD1 Stabilizes the Adsorption Vertex Structure
- The Small Viral Membrane-Associated Protein P32 Is Involved in Bacteriophage PRD1 DNA Entry