Bjorn M J, Vasil M L, Sadoff J C, Iglewski B H
Infect Immun. 1977 Apr;16(1):362-6. doi: 10.1128/iai.16.1.362-366.1977.
Pseudomonas aeruginosa exotoxin A has been shown to catalyze the transfer of the adenosine 5'-diphosphate (ADP)-ribose moiety of nicotinamide adenine dinucleotide onto elongation factor 2, resulting in the inhibition of mammalian protein synthesis. The enzymatic activity (ADP-ribosyl [ADPR]-transferase) is thought to account for the toxicity of exotoxin A. The distribution of the expression of exotoxin A within Pseudomonas species was examined. Laboratory strains as well as clinical isolates of Pseudomonas aeruginosa were tested. The production of exotoxin A was determined by assaying for ADPR-transferase activity in dialyzed frozen (-20 degrees C) and thawed cell-free supernatants from 22-h cultures or in 10-fold-concentrated supernatants. In addition, toxin production was detected immunologically using a modified Elek test. Exotoxin A production was detected in approximately 90% of the 111 isolates of P. aeruginosa. In contrast, none of the other species of Pseudomonas examined produced exotoxin A detectable by either ADPR-transferase activity or immunological reactivity.
铜绿假单胞菌外毒素A已被证明能催化烟酰胺腺嘌呤二核苷酸的腺苷5'-二磷酸（ADP）-核糖部分转移到延伸因子2上，从而抑制哺乳动物蛋白质合成。酶活性（ADP-核糖基[ADPR]转移酶）被认为是外毒素A毒性的原因。研究了外毒素A在假单胞菌属内的表达分布。对铜绿假单胞菌的实验室菌株和临床分离株进行了检测。通过测定来自22小时培养物的透析冷冻（-20℃）和解冻的无细胞上清液或10倍浓缩上清液中的ADPR转移酶活性来确定外毒素A的产生。此外，使用改良的Elek试验通过免疫学方法检测毒素产生。在111株铜绿假单胞菌分离株中，约90%检测到外毒素A产生。相比之下，所检测的其他假单胞菌属物种均未产生可通过ADPR转移酶活性或免疫反应性检测到的外毒素A。
