A 59 kiloDalton outer membrane protein of Salmonella typhimurium protects against oxidative intraleukocytic killing due to human neutrophils.
A 59 kiloDalton outer membrane protein of Salmonella typhimurium protects against oxidative intraleukocytic killing due to human neutrophils.
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鼠伤寒沙门氏菌的 59 kD 外膜蛋白可防止人中性粒细胞导致的白细胞内氧化杀伤。
DOI：
10.1111/j.1365-2958.1990.tb00595.x
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发表时间：
1990
影响因子：
3.6
通讯作者：
Spitznagel,JK
中科院分区：
文献类型：
--
作者：
Stinavage,PS;Martin,LE;Spitznagel,JK
我们分离出了一种鼠伤寒沙门氏菌 (ST) 突变体 JKS400，它缺乏表面暴露的外膜蛋白 (Omp) 的产生，并且对多形核白细胞 (PMN) 的氧化抗菌机制表现出高度敏感。该 Omp 在十二烷基硫酸钠聚丙烯酰胺凝胶电泳 (SDS-PAGE) 中以大约 59 千道尔顿 (kD) 迁移。我们发现，通过 P22 转导，产生蛋白质的能力和对氧化杀伤发挥野生型抗性的能力紧密相关。将 JKS400 与在 LT2 中的 Tn10 插入文库上生长的 P22(HT)Ht 噬菌体进行转导，产生了四环素抗性分离株，这些分离株已恢复野生型蛋白质生产。进一步的实验表明，蛋白质生产的恢复伴随着亲本对 PMN 杀伤的抗性表型的恢复以及对 H2O2 的野生型抗性的恢复。 Tn10 的图谱位置被确定为沙门氏菌染色体中的 96 分钟。该蛋白似乎充当毒力因子，促进鼠伤寒沙门氏菌 LT2 在中性粒细胞中的氧依赖性杀伤机制中生存的能力。
We have isolated aSalmonella 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 theSalmonellachromosome.This protein appears to behave as a virulence factor, promoting the capacity ofSalmonella typhimuriumLT2 to survive oxygen‐dependent killing mechanisms in neutrophils.