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本文引用的文献

1
Complement regulator-acquiring surface protein 1 of Borrelia burgdorferi binds to human bone morphogenic protein 2, several extracellular matrix proteins, and plasminogen.伯氏疏螺旋体补体调控蛋白获取表面蛋白 1 与人骨形态发生蛋白 2、几种细胞外基质蛋白和纤溶酶原结合。
J Infect Dis. 2010 Aug 15;202(3):490-8. doi: 10.1086/653825.
2
Borrelia burgdorferi BmpA is a laminin-binding protein.伯氏疏螺旋体BmpA是一种层粘连蛋白结合蛋白。
Infect Immun. 2009 Nov;77(11):4940-6. doi: 10.1128/IAI.01420-08. Epub 2009 Aug 24.
3
Borrelia burgdorferi RevA antigen binds host fibronectin.伯氏疏螺旋体RevA抗原与宿主纤连蛋白结合。
Infect Immun. 2009 Jul;77(7):2802-12. doi: 10.1128/IAI.00227-09. Epub 2009 Apr 27.
4
The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin.伯氏疏螺旋体外表面蛋白ErpX可结合哺乳动物层粘连蛋白。
Microbiology (Reading). 2009 Mar;155(Pt 3):863-872. doi: 10.1099/mic.0.024604-0.
5
Common and unique contributions of decorin-binding proteins A and B to the overall virulence of Borrelia burgdorferi.核心蛋白聚糖结合蛋白A和B对伯氏疏螺旋体整体毒力的共同及独特作用
PLoS One. 2008 Oct 3;3(10):e3340. doi: 10.1371/journal.pone.0003340.
6
Essential protective role attributed to the surface lipoproteins of Borrelia burgdorferi against innate defences.伯氏疏螺旋体表面脂蛋白对固有防御具有重要的保护作用。
Mol Microbiol. 2008 Jul;69(1):15-29. doi: 10.1111/j.1365-2958.2008.06264.x. Epub 2008 Apr 28.
7
Both decorin-binding proteins A and B are critical for the overall virulence of Borrelia burgdorferi.饰胶蛋白聚糖结合蛋白A和B对伯氏疏螺旋体的整体毒力都至关重要。
Infect Immun. 2008 Mar;76(3):1239-46. doi: 10.1128/IAI.00897-07. Epub 2008 Jan 14.
8
Borrelia burgdorferi inhibits human neutrophil functions.伯氏疏螺旋体抑制人类中性粒细胞功能。
Microbes Infect. 2008 Jan;10(1):60-8. doi: 10.1016/j.micinf.2007.10.004. Epub 2007 Oct 18.
9
Borrelia burgdorferi BBB07 interaction with integrin alpha3beta1 stimulates production of pro-inflammatory mediators in primary human chondrocytes.伯氏疏螺旋体BBB07与整合素α3β1的相互作用刺激原代人软骨细胞中促炎介质的产生。
Cell Microbiol. 2008 Feb;10(2):320-31. doi: 10.1111/j.1462-5822.2007.01043.x. Epub 2007 Sep 6.
10
Use of CFSE staining of borreliae in studies on the interaction between borreliae and human neutrophils.CFSE 染色法在疏螺旋体与人类中性粒细胞相互作用研究中对疏螺旋体的应用。
BMC Microbiol. 2006 Oct 18;6:92. doi: 10.1186/1471-2180-6-92.

格尔氏疏螺旋体、阿氏疏螺旋体和伯氏疏螺旋体（严格意义上）的 DbpA 和 B 对 decorin 的结合。

Decorin binding by DbpA and B of Borrelia garinii, Borrelia afzelii, and Borrelia burgdorferi sensu Stricto.

机构信息

Department of Medical Microbiology and Immunology, University of Turku, Kiinamyllynkatu 13, Turku, Finland.

出版信息

J Infect Dis. 2011 Jul 1;204(1):65-73. doi: 10.1093/infdis/jir207.

DOI:10.1093/infdis/jir207
PMID:21628660
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3307154/
Abstract

BACKGROUND

Decorin adherence is crucial in the pathogenesis of Lyme borreliosis. Decorin-binding proteins (Dbp) A and B are the adhesins that mediate this interaction. DbpA and B of Borrelia garinii, Borrelia afzelii, and Borrelia burgdorferi sensu stricto (ss) differ in their amino acid sequence, but little attention has been paid to the potential difference in their decorin binding.

METHODS

We expressed recombinant DbpA and DbpB of B. garinii, B. afzelii, and B. burgdorferi ss and studied their binding to decorin. We also generated recombinant Borrelia strains to study the role of DbpA and DbpB in the adhesion of live spirochetes to decorin and decorin-expressing cells. RESULTS. Recombinant DbpA of B. garinii and DbpB of B. garinii and B. burgdorferi ss showed strong binding to decorin, whereas DbpA of B. burgdorferi ss and both DbpA and DbpB of B. afzelii exhibited no or only minor binding activity. DbpA and DbpB of B. garinii and B. burgdorferi ss also supported the adhesion of whole spirochetes to decorin and decorin-expressing cells, whereas DbpA and DbpB of B. afzelii did not exhibit this activity.

CONCLUSIONS

Dbp A and B of B. garinii and B. burgdorferi ss mediate the interaction between the spirochete and decorin, whereas the same adhesins of B. afzelii show only negligible activity.

摘要

背景

聚集素结合是莱姆病发病机制中的关键。聚集素结合蛋白（Dbp）A 和 B 是介导这种相互作用的黏附素。伯氏疏螺旋体、阿菲波尔斯纳密螺旋体和伯氏疏螺旋体（ss）的 DbpA 和 B 在氨基酸序列上存在差异，但对它们与聚集素结合的潜在差异关注甚少。

方法

我们表达了伯氏疏螺旋体、阿菲波尔斯纳密螺旋体和伯氏疏螺旋体（ss）的重组 DbpA 和 DbpB，并研究了它们与聚集素的结合。我们还生成了重组博氏疏螺旋体菌株，以研究 DbpA 和 DbpB 在活螺旋体与聚集素和表达聚集素的细胞黏附中的作用。结果： 伯氏疏螺旋体的重组 DbpA 和伯氏疏螺旋体和伯氏疏螺旋体（ss）的 DbpB 显示出与聚集素的强烈结合，而伯氏疏螺旋体（ss）的 DbpA 和阿菲波尔斯纳密螺旋体的 DbpA 和 DbpB 则表现出没有或只有轻微的结合活性。伯氏疏螺旋体和伯氏疏螺旋体（ss）的 DbpA 和 DbpB 也支持整个螺旋体与聚集素和表达聚集素的细胞的黏附，而阿菲波尔斯纳密螺旋体的 DbpA 和 DbpB 则没有这种活性。

结论

伯氏疏螺旋体和伯氏疏螺旋体（ss）的 DbpA 和 B 介导螺旋体与聚集素之间的相互作用，而阿菲波尔斯纳密螺旋体的相同黏附素则表现出微不足道的活性。