A 59 KILODALTON OUTER-MEMBRANE PROTEIN OF SALMONELLA-TYPHIMURIUM PROTECTS AGAINST OXIDATIVE INTRALEUKOCYTIC KILLING DUE TO HUMAN NEUTROPHILS

We have isolated a Salmonella typhimurium (ST) mutant, JKS400, deficient in the production of a surface‐exposed outer membrane protein (Omp) and phenotypically hypersensitive to the oxidative antimicrobial mechanism of polymorphonuclear leukocytes (PMNs). This Omp migrated at approximately 59 kiloDaltons (kD) in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE). We found with P22 transduction that the capacities to produce the protein and to exert wild‐type resistance to oxidative killing were tightly linked. Transduction of JKS400 with a P22(HT)Ht bacteriophage grown on a Tn10 insertion library in LT2 yielded tetracycline‐resistant isolates that had been returned to wild‐type protein production. Further experiments showed that restoration of protein production was accompanied by restoration of the parental resistance phenotype to killing by PMNs and by restoration to wild‐type resistance to H2O2. The map position of the Tn10 was determined to be at 96 minutes in the Salmonella chromosome. This protein appears to behave as a virulence factor, promoting the capacity of Salmonella typhimurium LT2 to survive oxygen‐dependent killing mechanisms in neutrophils. Copyright © 1990, Wiley Blackwell. All rights reserved