Protein–lipid interactions of bacteriophage M13 major coat protein

Abstract

During the past years, remarkable progress has been made in our understanding of the replication cycle of bacteriophage M13 and the molecular details that enable phage proteins to navigate in the complex environment of the host cell. With new developments in molecular membrane biology in combination with spectroscopic techniques, we are now in a position to ask how phages carry out this delicate process on a molecular level, and what sort of protein-lipid and protein-protein interactions are involved. In this review we will focus on the molecular details of the protein-protein and protein-lipid interactions of the major coat protein (gp8) that may play a role during the infection of Escherichia coli by bacteriophage M13.

Anchoring mechanisms of membrane-associated M13 major coat protein

“…The recent progress in our understanding of anchoring mechanisms would not have been possible without a rapid development of protein engineering tools (Popot and Saraste, 1995). In particular, insertion of cysteine residues has been the basis for a great diversity of biochemical and biophysical experiments, ranging from the exploration of secondary, tertiary, and quaternary structures of transmembrane regions to the creation of site-specific points for spectroscopic reporter molecules (Hubbell et al, 1996;Hustedt and Beth, 1999;Liu et al, 2001;Mchaourab et al, 1997;Perozo et al, 2002;Stopar et al, 1996;Stopar et al, 2003;Štrancar et al, 2005). This review will illustrate the use of such tools to unravel several structural anchoring elements of membrane proteins by highlighting the specific protein-lipid interactions of the bacteriophage M13 major coat protein.…”

Mass Spectrometry of Nanoparticles is Different

“…This situation is illustrated with data obtained with Au 400 4+ impacts on the M13 bacteriophage. The specimen is filamentous, 900nm in length, 7-9nm in width, and encapsulates a circular single-stranded DNA [24]. Details of the characterization of individual M13 can be found in [25].…”

Thermodynamics of α-lactalbumin–dl-α-dipalmitoylphosphatidylcholine interactions and effect of the antioxidant nicotinamide on these interactions

“…Such systems are essential for understanding enzyme function, cellular communications [3][4][5], the mechanism of action of certain toxins, pathogens, protein insertion into membranes, and protein translocation across biological membranes [6]. Many reports are available in literature showing the interaction of lipid and proteins in a qualitative manner [3][4][5][6][7][8][9][10]. The conformational changes in proteins in the presence of lipids have also been extensively studied [7,9,10].…”

“…Many reports are available in literature showing the interaction of lipid and proteins in a qualitative manner [3][4][5][6][7][8][9][10]. The conformational changes in proteins in the presence of lipids have also been extensively studied [7,9,10]. However, quantitative studies on the lipid-protein interaction are generally rare.…”