The outer membrane protein TolC is required for phytoalexin resistance and virulence of the fire blight pathogen Erwinia amylovora.
The outer membrane protein TolC is required for phytoalexin resistance and virulence of the fire blight pathogen Erwinia amylovora.
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DOI：
10.1111/j.1751-7915.2009.00095.x
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发表时间：
2009-07
影响因子：
5.7
通讯作者：
Ullrich MS
中科院分区：
文献类型：
--
作者：
Al-Karablieh N;Weingart H;Ullrich MS
梨火疫病菌在苹果和梨等几种植物上引起火疫病，这些植物产生不同的植物抗毒素作为防御机制。因此，进化成功的病原体必须对这些有毒化合物产生抗性机制。急诊解淀粉菌外膜蛋白TolC可能通过与多药外排泵AcrAB相互作用介导植保素抗性。为了证明这一点，构建了tolC突变体和acrB/tolC双突变体。不同的抗菌剂和植物抗毒素的最低抑菌浓度测定这些突变体，并与以前产生的acrB突变体。tolC和arcB/tolC突变体比野生型敏感得多，但表现出与acrB突变体相似的水平。结果清楚地表明，无论是TolC或AcrAB显着相互作用与其他运输系统在流出的测试有毒化合物。对接种苹果的存活率和致病力测定表明，E. tolC和acrB/tolC突变同样削弱了食淀粉菌定殖植物组织的能力。我们的研究结果支持了TolC作为E.通过与AcrAB的专一性相互作用介导对植物抗毒素的抗性，从而抑制淀粉食心虫的生长。
Erwinia amylovora causes fire blight on several plant species such as apple and pear, which produce diverse phytoalexins as defence mechanisms. An evolutionary successful pathogen thus must develop resistance mechanisms towards these toxic compounds. The E. amylovora outer membrane protein, TolC, might mediate phytoalexin resistance through its interaction with the multidrug efflux pump, AcrAB. To prove this, a tolC mutant and an acrB/tolC double mutant were constructed. The minimal inhibitory concentrations of diverse antimicrobials and phytoalexins were determined for these mutants and compared with that of a previously generated acrB mutant. The tolC and arcB/tolC mutants were considerably more susceptible than the wild type but showed similar levels as the acrB mutant. The results clearly indicated that neither TolC nor AcrAB significantly interacted with other transport systems during the efflux of the tested toxic compounds. Survival and virulence assays on inoculated apple plants showed that pathogenicity and the ability of E. amylovora to colonize plant tissue were equally impaired by mutations of tolC and acrB/tolC. Our results allowed the conclusion that TolC plays an important role as a virulence and fitness factor of E. amylovora by mediating resistance towards phytoalexins through its exclusive interaction with AcrAB.
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