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首页> 外文期刊>Infection and immunity >Deletion of mtrC in Haemophilus ducreyi Increases Sensitivity to Human Antimicrobial Peptides and Activates the CpxRA Regulon
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Deletion of mtrC in Haemophilus ducreyi Increases Sensitivity to Human Antimicrobial Peptides and Activates the CpxRA Regulon

机译：ducreyi嗜血杆菌中mtrC的删除增加了对人类抗菌肽的敏感性并激活了CpxRA调节子。

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Haemophilus ducreyi resists killing by antimicrobial peptides encountered during human infection, including cathelicidin LL-37, α-defensins, and β-defensins. In this study, we examined the role of the proton motive force-dependent multiple transferable resistance (MTR) transporter in antimicrobial peptide resistance in H. ducreyi. We found a proton motive force-dependent effect on H. ducreyi's resistance to LL-37 and β-defensin HBD-3, but not α-defensin HNP-2. Deletion of the membrane fusion protein MtrC rendered H. ducreyi more sensitive to LL-37 and human β-defensins but had relatively little effect on α-defensin resistance. The mtrC mutant 35000HPmtrC exhibited phenotypic changes in outer membrane protein profiles, colony morphology, and serum sensitivity, which were restored to wild type by trans-complementation with mtrC. Similar phenotypes were reported in a cpxA mutant; activation of the two-component CpxRA regulator was confirmed by showing transcriptional effects on CpxRA-regulated genes in 35000HPmtrC. A cpxR mutant had wild-type levels of antimicrobial peptide resistance; a cpxA mutation had little effect on defensin resistance but led to increased sensitivity to LL-37. 35000HPmtrC was more sensitive than the cpxA mutant to LL-37, indicating that MTR contributed to LL-37 resistance independent of the CpxRA regulon. The CpxRA regulon did not affect proton motive force-dependent antimicrobial peptide resistance; however, 35000HPmtrC had lost proton motive force-dependent peptide resistance, suggesting that the MTR transporter promotes proton motive force-dependent resistance to LL-37 and human β-defensins. This is the first report of a β-defensin resistance mechanism in H. ducreyi and shows that LL-37 resistance in H. ducreyi is multifactorial.
机译：杜克雷嗜血杆菌抵抗人类感染期间遇到的抗菌肽（包括cathelicidin LL-37，α-防御素和β-防御素）的杀伤作用。在这项研究中，我们检查了质子原动力依赖的多重可转移抗性（MTR）转运蛋白在杜克氏杆菌的抗菌肽抗性中的作用。我们发现质子动力依赖于杜克雷伊菌对LL-37和β-防御素HBD-3的抗性，但对α-防御素HNP-2的抗性。膜融合蛋白MtrC的缺失使得杜克氏杆菌对LL-37和人β-防御素更加敏感，但对α-防御素的抵抗力相对较小。 mtrC突变体35000HPmtrC在外膜蛋白谱，菌落形态和血清敏感性方面表现出表型变化，并通过与mtrC反式互补而恢复为野生型。在cpxA突变体中报告了相似的表型。通过在35000HPmtrC中显示对CpxRA调控基因的转录效应，证实了两组分CpxRA调控物的激活。一个cpxR突变体具有野生型水平的抗菌肽耐药性。 cpxA突变对防御素的抵抗几乎没有影响，但导致对LL-37的敏感性增加。 35000HPmtrC比cpxA突变体对LL-37更加敏感，表明MTR有助于LL-37抗性，而与CpxRA规则无关。 CpxRA regulon不会影响质子动力依赖性抗菌肽的耐药性;然而，35000HPmtrC失去了质子动力依赖的肽抗性，表明MTR转运蛋白促进了对LL-37和人β-防御素的质子动力依赖的抗性。这是杜克氏菌中β-防御素耐药机制的首次报道，表明杜克氏菌中的LL-37耐药性是多因素的。

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