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Cystathionine β-Lyase Is Important for Virulence of Salmonella enterica Serovar Typhimurium

机译：胱硫醚β-裂解酶对肠炎沙门氏菌鼠伤寒沙门氏菌的致病性很重要

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摘要

The biosynthesis of methionine in bacteria requires the mobilization of sulfur from Cys by the formation and degradation of cystathionine. Cystathionine β-lyase, encoded by metC in bacteria and STR3 in Schizosaccharomyces pombe, catalyzes the breakdown of cystathionine to homocysteine, the penultimate step in methionine biosynthesis. This enzyme has been suggested to be the target for pyridinamine antimicrobial agents. We have demonstrated, by using purified enzymes from bacteria and yeast, that cystathionine β-lyase is not the likely target of these agents. Nonetheless, an insertional inactivation of metC in Salmonella enterica serovar Typhimurium resulted in the attenuation of virulence in a mouse model of systemic infection. This result confirms a previous chemical validation of the Met biosynthetic pathway as a target for the development of antibacterial agents and demonstrates that cystathionine β-lyase is important for bacterial virulence.
机译：细菌中蛋氨酸的生物合成需要通过胱硫醚的形成和降解来从Cys中迁移出硫。细菌中 metC 和 Schizosaccharomyces pombe 中的 STR3 编码的胱硫醚β-裂合酶催化胱硫醚分解为高半胱氨酸，这是蛋氨酸的倒数第二个步骤生物合成。该酶已被认为是吡啶胺抗微生物剂的靶标。我们已经证明，通过使用来自细菌和酵母的纯化酶，胱硫醚β-裂合酶不是这些药物的靶标。尽管如此，在沙门氏菌血清鼠伤寒沙门氏菌中 metC 的插入失活导致系统性感染小鼠模型的毒力减弱。该结果证实了Met生物合成途径作为抗菌剂开发目标的先前化学验证，并证明胱硫醚β-裂合酶对于细菌毒力很重要。

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