Biological activity of fragments derived from the extracellular slime glycolipoprotein of Pseudomonas aeruginosa.

Glycolipoprotein, obtained from the extracellular slime layer of Pseudomonas aeruginosa, was purfied and subjected to chemical and enzymatic treatment in an attempt to assign certain of its biological activities to chemical moieties comprising the glycolipoprotein molecule. Treatment of the glycolipoprotein with phenol, although removing all detectable protein, yielded a fragment capable to exerting the biological activities associated with the untreated glycolipoprotein (leucopenia, lethality, inhibition of phagocytosis, antigenic specificity). Acetic acid treatment resulted in a fragment composed mainly of carbohydrate and a small amount of protein, but no detectable lipid. This fragment was devoid of leucopenic and lethal activity, but retained antigenic specificity and the ability to inhibit phagocytosis. The fragments release from the glycolipoprotein after treatment with phage 2-depolymerase were low-molecular-weight products and were devoid of the biological activities associate with the glycolipoprotein.