Studies on the Bacterial Surface Structure of Gram-negative Bacteria and its Biological Active Substances

Abstract

The simple protein (LSAS) was isolated from the cell wall of Pseudomonas aeruginosa, A (α) strain. It is a higher molecular weight substance than the protein fraction (Orig. endot.-P) of the “Original endotoxin” which is isolated from the autolysate. Both proteins have the same potency in pyocine activity and the identical spectrum against sensible strains.The LSAS anti-serum can neutralizeα, a lysogenic phage of A (α), against various kinds of the sensible strains. However, Original endotoxin and Orig. endot.-P anti-sera can not neutralize phageαagainst some of the sensible strains. The lipopolysaccharide anti-serum can not neutralize phageαagainst any kind of sensible strains.Double lysogenic strain RV (α2, δ) was obtained when a lysogenic strain R (δ) was infected with Phage a of A (α) strain. From the results of phage neutralizing test and pyocine neutralizing test usingα, α2, LSAS, Orig. endot.-P and their sera, it was found that the protein envelope of lysogenic phageα2had some of the common serological specificities of the protein moieties (LSAS, Orig. endot.-P) of the endotoxin and the protein envelope of phage a. The results are same in another experiment using a system of A (α), E (β), and EV (α1, β) strains.Considering these results, it may be said that the protein envelope of a lysogenic phage contains all or some of the protein moiety of the endotoxin in the cell wall. A strain E (β) is infected with an another kind of a lysogenic phage a and a double lysogenic strain EV (α1, β) is obtained. The protein envelope of the lysogenic phageα1has the common serological specificity with the cell wall protein of the strain A (α).