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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Targeted mutation of the outer membrane protein P66 disrupts attachment of the Lyme disease agent, Borrelia burgdorferi, to integrin alpha(v)beta(3)
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Targeted mutation of the outer membrane protein P66 disrupts attachment of the Lyme disease agent, Borrelia burgdorferi, to integrin alpha(v)beta(3)

机译：外膜蛋白P66的有针对性的突变破坏了莱姆病病菌伯氏疏螺旋体对整联蛋白α（v）beta（3）的附着

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摘要

Borrelia burgdorferi, the agent of Lyme disease, expresses several adhesion molecules that are probably required for initial establishment of infection in mammalian hosts, and for colonization of various tissues within the host. The B. burgdorferi outer membrane protein P66 was previously identified as a ligand for beta(3)-chain integrins by using a variety of biochemical approaches.' Although the earlier data suggested that P66 is an adhesin that mediates B. burgdorferi attachment to beta(3)-chain integrins, lack of genetic systems in B. burgdorferi precluded definitive demonstration of a role for P66 in beta(3) integrin attachment by intact borreliae. Recent advances in the genetic manipulation of B. burgdorferi have now made possible the targeted disruption of the p66 gene. Mutants in p66 show dramatically reduced attachment to integrin alpha(v)beta(3). This is, to our knowledge, the first description of the targeted disruption of a candidate B. burgdorferi virulence factor with a known biochemical function that can be quantified, and demonstrates the importance of B. burgdorferi P66 in the attachment of this pathogenic spirochete to a human cell-surface receptor. [References: 34]
机译：伯氏疏螺旋体是莱姆病的病原，它表达了几种粘附分子，这可能是哺乳动物宿主最初建立感染以及宿主内各种组织定植所必需的。通过使用多种生化方法，先前已将伯氏疏螺旋体外膜蛋白P66鉴定为β（3）-链整联蛋白的配体。尽管较早的数据表明P66是一种介导B. burgdorferi附着于β（3）链整合素的粘附素，但由于B. burgdorferi中缺乏遗传系统，因此无法确定P66在β（3）整合素附着中的作用是完整的紫菜。 B. burgdorferi的基因操作方面的最新进展现已使p66基因的定向破坏成为可能。 p66中的突变体显示与整合素alpha（v）beta（3）的附着力大大降低。据我们所知，这是对具有已知生化功能且可量化的候选伯氏疏螺旋体毒力因子的靶向破坏的首次描述，并证明了伯氏疏螺旋体P66在该致病性螺旋体附着于细菌中的重要性。人细胞表面受体。 [参考：34]

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