Dec 1, 1989

O antigen and lipid A phosphoryl groups in resistance of Salmonella typhimurium LT-2 to nonoxidative killing in human polymorphonuclear neutrophils

Infection and Immunity
P StinavageJ K Spitznagel

Abstract

We have compared the intraleukocytic survival of isogenic strains of Salmonella typhimurium, whose outer membrane lipopolysaccharide differed in O antigen and lipid A composition and whose susceptibility to nonoxidative antimicrobial granule proteins of human polymorphonuclear neutrophilis (PMN) could be established. We found that the order of resistance to the bactericidal activity of intact PMN of the three bacterial strains utilized closely resembled their ordered resistance to the purified human cationic antimicrobial 57,000-dalton protein (CAP57). LT-2, a smooth wild-type strain, was far more resistant than SH9178, its rough (Rb LPS) mutant. It was most significant that SH7426, a polymyxin B-resistant pmrA mutant of SH9178, not only was substantially more resistant to CAP57 and to intraphagocytic killing than SH9178 but also came close to being as resistant as LT-2. These experiments confirm earlier work that showed the importance of the glycosyl groups of O antigens of S. typhimurium for their resistance to O2-independent antimicrobial phagocytosis by PMN. The surprising result was that a rough strain, very susceptible to bactericide, became substantially more resistant when a mutation led to its lipid A phosphoryl groups...Continue Reading

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Mentioned in this Paper

Bactericide, NOS
Neutrophil Band Cells
Outer Membrane
Structure-Activity Relationship
Serum Proteins
Pentoses
Bactericidal Activity
Cationic antimicrobial protein 57, human
Antigens, Bacterial
Genes, Bacterial

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