Studies of a receptor for FP3-phage in Salmonella minnesota R595.

The adsorption rate constant of the phage FP3 to sensitive S. minnesota R595 strain was used to evaluate the inactivating capacity towards phage FP3 exhibited by isolated glycolipid and free lipid A. The results suggest that phage FP3 receptor is localized in the glycolipid structure. Phage FP3 is not adsorbed on the other Re mutant cells, Proteus R45, but respective products: glycolipid and free lipid A from R45 exhibitory the inhibition capacity towards phage FP3, comparable to the activity of the products derived from the host strain; the minimal PhI50 concentration of glycolipids is 7.8 and 15.6 microgram/ml respectively.