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疏螺旋体属中的糖蛋白模式

Glycoprotein patterns in Borrelia spp.

作者信息

Sambri V, Massaria F, Ardizzoni M, Stefanelli C, Cevenini R

机构信息

Institute of Microbiology, University of Bologna, S. Orsola Hospital, Italy.

出版信息

Zentralbl Bakteriol. 1993 Aug;279(3):330-5. doi: 10.1016/s0934-8840(11)80365-8.

DOI:10.1016/s0934-8840(11)80365-8
PMID:8219503
Abstract

The presence of glycoproteins in several Borrelia species was investigated by the digoxigenin labelling technique. The outer surface proteins A and B of seven isolates of the Lyme disease spirochete B. burgdorferi showed to be major glycosylated proteins. Few minor polypeptides with variable molecular masses were also present, at variance, in B. burgdorferi strains. Minor glycosylated proteins with varying molecular masses have been detected in the relapsing fever borreliae B. hermsii, B. turicatae and B. parkeri. B. turicatae showed also a major glycosylated protein with a molecular mass of approximately 40 kDa. Animal pathogenic borreliae B. anserina and B. coriaceae presented only minor glycosylated proteins with variable molecular masses.

摘要

采用地高辛标记技术研究了几种疏螺旋体中糖蛋白的存在情况。莱姆病螺旋体伯氏疏螺旋体的七个分离株的外表面蛋白A和B显示为主要的糖基化蛋白。不同的伯氏疏螺旋体菌株中还存在少数分子量可变的次要多肽。在回归热疏螺旋体赫氏疏螺旋体、土拉疏螺旋体和帕克疏螺旋体中检测到了分子量不同的次要糖基化蛋白。土拉疏螺旋体还显示出一种分子量约为40 kDa的主要糖基化蛋白。动物致病性疏螺旋体鹅疏螺旋体和科氏疏螺旋体仅呈现分子量可变的次要糖基化蛋白。

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Glycoprotein patterns in Borrelia spp.疏螺旋体属中的糖蛋白模式
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2
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A surface-exposed region of a novel outer membrane protein (P66) of Borrelia spp. is variable in size and sequence.疏螺旋体属一种新型外膜蛋白(P66)的表面暴露区域在大小和序列上存在差异。
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Structural analysis of an outer surface protein from the Lyme disease spirochete, Borrelia burgdorferi, using circular dichroism and fluorescence spectroscopy.利用圆二色光谱和荧光光谱对莱姆病螺旋体伯氏疏螺旋体的一种外表面蛋白进行结构分析。
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A murine IgG1 monoclonal antibody that binds specifically to outer surface protein A of Lyme disease spirochete Borrelia burgdorferi.一种鼠源IgG1单克隆抗体,它能特异性结合莱姆病螺旋体伯氏疏螺旋体的外表面蛋白A。
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Evidence of involvement of the mannose receptor in adhesion of Borrelia burgdorferi to monocyte/macrophages.甘露糖受体参与伯氏疏螺旋体与单核细胞/巨噬细胞黏附的证据。
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