The BB0646 protein demonstrates lipase and haemolytic activity associated with Borrelia burgdorferi, the aetiological agent of Lyme disease.
The BB0646 protein demonstrates lipase and haemolytic activity associated with Borrelia burgdorferi, the aetiological agent of Lyme disease.
复制标题
BB0646 蛋白表现出与伯氏疏螺旋体(莱姆病的病原体)相关的脂肪酶和溶血活性。
DOI:
10.1111/j.1365-2958.2011.07932.x
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发表时间:
2012
影响因子:
3.6
通讯作者:
Skare,JonT
中科院分区:
文献类型:
--
作者:
Shaw,DanaK;Hyde,JennyA;Skare,JonT
The etiological agent of Lyme disease,Borrelia burgdorferi, is transmitted by ticks of theIxodesgenus and, if untreated, can cause significant morbidity in affected individuals. Recent reports have shown that polyunsaturated fatty acids in theB. burgdorfericell envelope are potential targets for oxidative damage, which can be lethal. HowB. burgdorferiresponds to this assault is not known. Herein we report evidence thatbb0646codes for a lipase that is located within thebosRoperon and that has specificity for both saturated and polyunsaturated fatty acids. Specifically, strains harbouring mutated copies of the lipase, either in the form of an insertionally inactivated construct or site‐directed mutations within the active site, demonstrated attenuated lipolytic and haemolytic phenotypes when compared with the isogenic parent andtrans‐complements.In vivoanalysis showed that while thebb0646mutant remains infectious, the spirochaetal load is significantly lower than both the isogenic parent and the complemented mutant strains. Taken together, these data demonstrate that BB0646 is a broad substrate specific lipase that contributes to lipolytic and haemolytic activityin vitroand is required for optimalB. burgdorferiinfection.