Gemmell C G
J Med Microbiol. 1984 Jun;17(3):217-35. doi: 10.1099/00222615-17-3-217.
It is apparent that there are considerable similarities between many of the enterotoxins produced by enteric pathogens. Although the effect of most of these toxins is restricted to the intestine in vivo, many cells are also sensitive to intoxication in vitro. The resultant in-vitro biochemical changes may have no pathological significance but serve to underline the central role of cyclic nucleotides in cellular fluid regulation. The biological activity of these enterotoxins is the result of interaction with membrane-bound adenylate cyclase, leading to persistent elevation of intracellular levels of cAMP. Stimulation of adenylate cyclase occurs consistently after a characteristic lag phase which varies somewhat between toxins. The duration and degree of stimulation of adenylate cyclase by the various toxins may point to possible differences in affinity, dissociation and mechanism of activation of the cyclase molecule. Subtle events at, or within, the cell membrane must occur during intoxication and may include complex associations of toxin with membrane lipid and protein components. The heat-labile toxins of V. cholerae, E. coli, Salmonella spp., A. hydrophila and Y. enterocolitica have much in common in their structures, membrane receptors and biochemical modes of action. Similarly the heat-stable toxins of E. coli and Y. enterocolitica, match each other in their biological activities. Classified along with the enterotoxin of C. perfringens, the enterotoxin produced by Sh. dysenteriae (and possibly some strains of E. coli) appears to differ from the other enterotoxins by acting on protein biosynthesis primarily and not on the nucleotide cyclase activation systems. In another category must be placed the various enterotoxins produced by Staph. aureus until more is known. Surprisingly little research has been directed towards the elucidation of their mode of action, although much is known of their serological and structural differences. Evidence to date suggests that staphylococcal enterotoxins differ from the other diarrhoeagenic agents discussed in this review. The structural and immunological similarities between the various heat-labile enterotoxins suggest a common genetic origin with gene transfer between the different bacterial species being responsible for the spread of enterotoxigenicity. It is possible that many of the "newer" enterotoxins owe their origin to genetic recombination with the "older" enteropathogens like V. cholerae.
显然,许多肠道病原体产生的肠毒素之间存在相当多的相似之处。虽然这些毒素中的大多数在体内的作用仅限于肠道,但许多细胞在体外也对毒素中毒敏感。由此产生的体外生化变化可能没有病理意义,但有助于强调环核苷酸在细胞液调节中的核心作用。这些肠毒素的生物活性是与膜结合的腺苷酸环化酶相互作用的结果,导致细胞内cAMP水平持续升高。腺苷酸环化酶的刺激在特征性的延迟期后持续发生,不同毒素之间的延迟期略有不同。各种毒素对腺苷酸环化酶的刺激持续时间和程度可能表明环化酶分子在亲和力、解离和激活机制上可能存在差异。在中毒过程中,细胞膜上或细胞膜内必定发生了微妙的事件,可能包括毒素与膜脂质和蛋白质成分的复杂结合。霍乱弧菌、大肠杆菌、沙门氏菌属、嗜水气单胞菌和小肠结肠炎耶尔森菌的不耐热毒素在结构、膜受体和生化作用模式上有很多共同之处。同样,大肠杆菌和小肠结肠炎耶尔森菌的耐热毒素在生物活性上相互匹配。与产气荚膜梭菌的肠毒素归为一类,痢疾志贺菌(可能还有一些大肠杆菌菌株)产生的肠毒素似乎与其他肠毒素不同,它主要作用于蛋白质生物合成,而不是核苷酸环化酶激活系统。在更多信息被了解之前,金黄色葡萄球菌产生的各种肠毒素必须归为另一类。令人惊讶的是,尽管对它们的血清学和结构差异了解很多,但针对阐明其作用方式的研究却很少。迄今为止的证据表明,葡萄球菌肠毒素与本综述中讨论的其他致泻剂不同。各种不耐热肠毒素之间的结构和免疫学相似性表明它们有共同的遗传起源,不同细菌物种之间的基因转移导致了产肠毒素性的传播。许多“新型”肠毒素可能起源于与霍乱弧菌等“古老”肠道病原体的基因重组