Role of lipopolysaccharide and outer membrane protein of Escherichia coli K-12 in the receptor activity for bacteriophage T4.
Lipopolysaccharide isolated from Escherichia coli K-12 did not inactivate phage T4, although the cell envelopes with 1% sodium deoxycholate resulted in the release of cytoplasmic membrane proteins, 70% of the lipopolysaccharide, and almost all of the phospholipid. The reconstitution of phage receptor activity was achieved from deoxycholate-soluble and -insoluble fractions by dialysis against a solution of magnesium chloride. Lipopolysaccharide was the only essential component in the deoxycholate-soluble fraction. PhageT4-resistant mutants YA21-6 and YA21-82, having defects in the deoxycholate-soluble and -insoluble fractions, respectively, were isolated. The deoxycholate-soluble fraction of YA21-6 possessed heptoseless lipopolysaccharide, and this defect was responsible for the phage resistance. The deoxycholate-insoluble fraction of YA21-82 lacked outer membrane protein O-8. The addition of O-8 to this fraction together with the wild-type lipopolysaccharide resulted in the appearance of the receptor activity. Furthermore, the reconstitution was successfully achieved with only O-8 and the wild-type lipopolysaccharide, indicating that O-8 was an essential component in the deoxycholate-insoluble fraction.
D001426:Bacterial Proteins / Q000502:physiology*; D003090:Coliphages; D003840:Deoxycholic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000032:analysis / Q000502:physiology*; D008070:Lipopolysaccharides / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology*; D011991:Receptors, Virus / Q000502:physiology*
D001426:Bacterial Proteins; D008070:Lipopolysaccharides; D008565:Membrane Proteins; D011991:Receptors, Virus; D003840:Deoxycholic Acid