The lethal moiety of the surface slime glycolipoprotein ofPseudomonas aeruginosa

Phenol treatment of the glycolipoprotein fromPseudomonas aeruginosa, followed by gel filtration and anion-exchange chromatography, produced a glycolipid fragment free of protein. A second, lipid-rich fragment was obtained as a precipitate of dilute acetic-acid hydrolysis of the glycolipoprotein. After solubilization, the lipid-rich fragment was processed on Sephadex G-200. Both lipid-containing fragments were immunologically homogeneous in Ouchterlony plates against rabbit antiserum to crude glycolipoprotein. The precipitin bands indicated that polysaccharide residues conferred the antigenic specificity. General chemical analyses were made on each fragment. All lipid-containing fragments were lethal, to varying degrees, on injection in mice. Proteinase K digestion of the glycolipoprotein did not reduce its lethality. All lipid-containg fragments stimulated varying levels of antibody capable of passively protecting mice against lethal challenge with viablePseudomonas aeruginosa. The contribution of the carbohydrate moiety to the expression of lethality is discussed.