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首页> 外文期刊>Infection and immunity >Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa.
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Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa.

机译：比较对铜绿假单胞菌有杀菌作用的人多形核白细胞颗粒蛋白。

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Killing of Pseudomonas aeruginosa by a 55-kDa bactericidal protein (BP 55), a 30-kDa protein (BP 30), cathepsin G, elastase, and proteinase 3 has been compared. P. aeruginosa was resistant to killing by elastase and proteinase 3. BP 55 at a 50% lethal dose (LD50) of 0.23 micrograms of protein per 5 x 10(6) bacteria per ml killed P. aeruginosa and was far more active than BP 30 and cathepsin G. The LD50s of BP 30 and cathepsin G were 16.9 and 28.3 micrograms of protein per 5 x 10(6) bacteria per ml, respectively. Preincubation of BP 55 or BP 30 with lipopolysaccharide (LPS) from P. aeruginosa inhibited bactericidal activity. The N-terminal amino acid sequence of BP 55 and BP 30 revealed no relationship between the two proteins. However, a monoclonal antibody (AHN-15) reacted with both proteins by Western immunoblot. The bactericidal activity of cathepsin G toward P. aeruginosa appeared to be dependent on the availability of the active site of the enzyme; bactericidal activity was inhibited by phenylmethylsulfonyl fluoride (PMSF) and by the specific cathepsin G inhibitor, Z-Gly-Leu-Phe-CH2Cl. The enzyme and bactericidal activities of cathepsin G were also inhibited by LPS from P. aeruginosa. LPS from P. aeruginosa was shown to be a competitive inhibitor of the enzyme activity of cathepsin G. Elastase enzyme activity was also inhibited noncompetitively by LPS, but the enzyme was not bactericidal. We have concluded that all three bactericidal proteins (BP 55, BP 30, and cathepsin G) may bind to the LPS of the outer membrane of P. aeruginosa. It appears that the enzyme active site must be available for cathepsin G to kill P. aeruginosa and that the active site may be involved in the binding of cathepsin G to P. aeruginosa.
机译：比较了55 kDa杀菌蛋白（BP 55），30 kDa蛋白（BP 30），组织蛋白酶G，弹性蛋白酶和蛋白酶3对铜绿假单胞菌的杀灭作用。铜绿假单胞菌对弹性蛋白酶和蛋白酶3的杀灭具有抗性30和组织蛋白酶G。每毫升5 x 10（6）细菌的BP 30和组织蛋白酶G的LD50分别为16.9和28.3微克蛋白质。用铜绿假单胞菌的脂多糖（LPS）对BP 55或BP 30进行预温育可抑制其杀菌活性。 BP 55和BP 30的N端氨基酸序列显示这两种蛋白之间没有关系。但是，单克隆抗体（AHN-15）通过Western免疫印迹与两种蛋白反应。组织蛋白酶G对铜绿假单胞菌的杀菌活性似乎取决于该酶活性位点的可用性。苯甲基磺酰氟（PMSF）和特定的组织蛋白酶G抑制剂Z-Gly-Leu-Phe-CH2Cl抑制了细菌的杀菌活性。组织蛋白酶G的酶和杀菌活性也被铜绿假单胞菌的LPS抑制。铜绿假单胞菌的LPS被证明是组织蛋白酶G酶活性的竞争性抑制剂。弹性蛋白酶的活性也被LPS非竞争性地抑制，但该酶没有杀菌作用。我们得出的结论是，所有三种杀菌蛋白（BP 55，BP 30和组织蛋白酶G）都可能与铜绿假单胞菌外膜的LPS结合。看来该酶活性位点对于组织蛋白酶G必不可少，以杀死铜绿假单胞菌，并且该活性位点可能参与了组织蛋白酶G与铜绿假单胞菌的结合。

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