A comparative study of Bacillus cereus, Bacillus thuringiensis and Bacillus anthracis extracellular proteomes
A comparative study of Bacillus cereus, Bacillus thuringiensis and Bacillus anthracis extracellular proteomes
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DOI：
10.1002/pmic.200401225
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发表时间：
2005-09-01
期刊：
影响因子：
3.4
通讯作者：
Lereclus, D
中科院分区：
文献类型：
--
作者：
Gohar, M;Gilois, N;Lereclus, D
蜡样芽孢杆菌、苏云金芽孢杆菌和炭疽芽孢杆菌是密切相关的物种，具有相似的遗传背景，但占据不同的生态位。携带毒素编码基因的毒力质粒可以至少部分地解释这种特殊性。我们通过 2DE 比较了这些物种中失去毒力质粒的三个菌株在生长早期稳定期的细胞外蛋白质组。在这三个蛋白质组中发现了预期被分泌或属于细胞壁或细胞质的蛋白质。对于位于细胞外空间的细胞壁和胞质蛋白，这三种蛋白质组是相似的。胞浆蛋白包括烯醇化酶、GroEL、PdhB、PdhD、SodA 等。细胞表面蛋白主要有自溶素、蛋白酶、核苷酸酶和OppAs。相反，蜡状芽孢杆菌和苏云金芽孢杆菌的分泌蛋白谱与炭疽芽孢杆菌有很大不同。蜡样芽孢杆菌和苏云金芽孢杆菌胞外蛋白质组均含有大量分泌的降解酶和毒素，包括九种蛋白酶、三种磷脂酶、两种溶血素和几种肠毒素。大多数编码这些酶和毒素的基因均由转录激活因子 PlcR 控制。 pXO1(-)、pXO2(-) B. anthracis 9131 菌株的胞外蛋白质组仅含有一种分泌蛋白：金属蛋白酶 InhA1，它也存在于其他两种菌株的蛋白质组中，并且可能参与抗菌肽降解。
Bacillus cereus, Bacillus thuringiensis and Bacillus anthracis are closely related species that share a similar genetic background but occupy different ecological niches. Virulence plasmids bearing genes coding for toxins, may explain, at least partly, this specialization. We have compared by 2DE in the early stationary phase of growth the extracellular proteomes of three strains of these species that have lost their virulence plasmids. Proteins expected to be secreted or to belong to the cell wall or to the cytosol were found in the three proteomes. For the cell wall and cytosolic proteins located in the extracellular space, the three proteomes were similar. Cytosolic proteins included enolase, GroEL, PdhB, PdhD, SodA and others. Cell surface proteins were mainly autolysins, proteases, nucleotidases and OppAs. In contrast, the secreted proteins profiles of B. cereus and B. thuringiensis were quite different from that of B. anthracis. B. cereus and B. thuringiensis extracellular proteomes both contained large amounts of secreted degradative enzymes and toxins, including nine proteases, three phospholipases, two haemolysins and several enterotoxins. Most of the genes encoding these enzymes and toxins are controlled by the transcriptional activator PlcR. The extracellular proteome of the pXO1(-), pXO2(-) B. anthracis 9131 strain contained only one secreted protein: the metalloprotease InhA1, also found in the proteomes of the two other strains and possibly involved in antibacterial peptide degradation.