Structure and synthesis of a lipid-containing bacteriophage. Purification, chemical composition, and partial...

The four structural proteins of the lipid-containing bacteriophage PM2 have been purified by dissociation of the virus in the presence of acetic acid followed by a combination of gel filtration and ion-exchange chromatography in the presence of sodium dodecylsulfate and guanidine hydrochloride. Amino acid analyses of each of the proteins were performed and correlated with the properties and functions of the proteins. Protein I has the highest polarity and is the only water-soluble protein. Protein II has a rather high polarity and hydrophobicity index and probably interacts electrostatically and hydrophobically with the bilayer. Proteins III and IV have low polarities and possess the solubility properties of proteolipids. At least protein III and perhaps also protein IV may interact with the bilayer. No fatty acids are covalently linked to these proteins. Tryptic fingerprints showed that proteins I and II contain a high proportion of hydrophobic peptides, but especially protein I also contains a large number of hydrophilic peptides. Proteins III and IV have relatively few hydrophobic peptides despite their relatively high hydrophobicity. Protein IV has two distinct regions, as shown by partial sequence studies. Basic amino acids at the N-terminus would serve for interaction with the viral DNA, the following hydrophobic sequence might interact with protein III or with the bilayer.