Lipid Selection in the Assembly of the Phospholipid Bilayer Membrane of the Lipid-Containing Bacteriophage PR4

doi:10.1006/viro.1994.1004

Virology

Volume 198, Issue 1, January 1994, Pages 25-30

https://doi.org/10.1006/viro.1994.1004 Get rights and content

Abstract

Phage PR4 contains a lipid bilayer within the phage protein capsid. The phospholipids of the bilayer are derived from those of the host. We report that phage morphogenesis selects against the unusually bulky phospholipids synthesized by Escherichia coli grown in the presence of various sugar alcohols. These data indicate that assembly of the PR4 lipid bilayer is a selective process rather than the bulk appropriation of host membrane lipids. We also demonstrate that phage PR4 morphogenesis is compatible with the incorporation of several abnormal lipids, monoacylglycerol, diacylglycerol, and phosphatidylinositol into the phage particle.

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Cited by (4)

Structure, interactions and dynamics of PRD1 virus II. Organization of the viral membrane and DNA
1996, Journal of Molecular Biology
Structure, dynamics and stability of the membrane and double-stranded (ds) DNA genome packaged within the nativePRD1virion have been probed by laser Raman spectroscopy. The Raman signature ofPRD1is complex, but exhibits distinctive marker bands diagnostic of the internal lipid bilayer and dsDNA. The Raman markers demonstrate, respectively, a liquid crystalline lipid phase (L_α) and aBDNA conformation throughout the temperature range (5°C to 50°C) of virion stability. Despite the absence of large scale lipid phase transitions or DNA melting, small temperature- dependent changes in the Raman markers of lipid and DNA are detected, indicating coupling between their structures. Minor deviations of DNA from the canonicalBform are imposed by the membrane. The Raman markers indicate further that base stacking and phosphate group interactions of the packagedPRD1genome differ from those of unpackagedPRD1DNA. Specific Raman band perturbations are proposed as indicators of DNA – membrane interaction. Hydrogen-deuterium exchange kinetics of packaged and unpackagedPRD1DNA are indistinguishable, demonstrat ing that base imino and amino protons are not affected significantly by either the condensation or membrane enclosure associated with DNA packaging. This contrasts with the significant acceleration of base exchanges detected in the packaged DNA of bacteriophageP22, which lacks a viral membrane. The distinctive H→²H exchange profile of thePRD1genome, the absence of packaging-induced acceleration of exchange kinetics and the apparent direct interaction between DNA and phospholipids suggest a specific role for the viral membrane inPRD1assembly. We propose a "membrane-surface-catalyzed" model for dsDNA condensation and organization within thePRD1virion.
Bacteriophage Prd1: A broad host range dsdna tectivirus with an internal membrane
1995, Advances in Virus Research
The widely used phage isolation method, described in Adams, includes a chloroform treatment step. As a result, bacterial viruses have been considered to be nucleic acid-protein assemblies. The omission of the organic solvent treatment from the isolation process resulted in the isolation of phages that also had a membrane component. The Tectiviridae are one of the most common phage groups containing a biological membrane. The Tectiviridae are divided into two subgroups, those infecting gram-positive and those infecting gram-negative hosts. The type organism for the gram-negative subgroup is PRD1, the other isolates being PR3, PR4, PR5, L17, and PR772. The best studied members of this virus group are PRD1 and PR4, and information given in this review is based mostly on the results obtained with these two virus systems. A comprehensive description on the current knowledge on PRD1 and related viruses are given in this chapter. Two characteristics, in particular, have drawn attention to the PRD1-type viruses: (1) the virion has an outer rigid protein capsid, inside of which resides a membrane that follows the internal capsid surface. (2) the viral genome is a linear dsDNA molecule that has a covalently linked protein at the 5' ends and inverted terminal repeat (ITR) sequences at both termini.
Integral membrane protein P16 of bacteriophage PRD1 stabilizes the adsorption vertex structure
2004, Journal of Virology
The assembly factor P17 from bacteriophage PRD1 interacts with positively charged lipid membranes
2000, European Journal of Biochemistry

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Virology

Regular ArticleLipid Selection in the Assembly of the Phospholipid Bilayer Membrane of the Lipid-Containing Bacteriophage PR4

Abstract

Structure, interactions and dynamics of PRD1 virus II. Organization of the viral membrane and DNA

Bacteriophage Prd1: A broad host range dsdna tectivirus with an internal membrane

Integral membrane protein P16 of bacteriophage PRD1 stabilizes the adsorption vertex structure

The assembly factor P17 from bacteriophage PRD1 interacts with positively charged lipid membranes

Regular Article
Lipid Selection in the Assembly of the Phospholipid Bilayer Membrane of the Lipid-Containing Bacteriophage PR4