Gassmann G S, Jacobs E, Deutzmann R, Göbel U B
Institut für Medizinische Mikrobiologie und Hygiene, Freiburg, Federal Republic of Germany.
J Bacteriol. 1991 Feb;173(4):1452-9. doi: 10.1128/jb.173.4.1452-1459.1991.
The fla gene of Borrelia burgdorferi GeHo was analyzed and expressed in Escherichia coli. The structural gene encodes a flagellar protein of 336 amino acids. Comparative sequence analysis of the amino acid sequence revealed a high degree of sequence conservation with flagellins from both phylogenetically related and unrelated bacteria. The antigenic properties of the B. burgdorferi Fla protein were studied by synthesizing overlapping octapeptides, which were screened by using a battery of different monoclonal and polyclonal antibodies from various species directed against native and denatured flagellar proteins. No single species-independent immunodominant epitope could be located. However, immunoreactive oligopeptides clustered within the variable middle region (N-180 to I-260). This region could constitute a candidate antigen for more specific and sensitive serodiagnosis of Lyme borreliosis.
对伯氏疏螺旋体GeHo株的fla基因进行了分析,并在大肠杆菌中进行了表达。该结构基因编码一种由336个氨基酸组成的鞭毛蛋白。对氨基酸序列进行的比较序列分析表明,其与来自系统发育相关和不相关细菌的鞭毛蛋白具有高度的序列保守性。通过合成重叠八肽研究了伯氏疏螺旋体Fla蛋白的抗原特性,这些八肽使用一系列来自不同物种的针对天然和变性鞭毛蛋白的不同单克隆和多克隆抗体进行筛选。未发现单一的不依赖物种的免疫显性表位。然而,免疫反应性寡肽聚集在可变的中间区域(N-180至I-260)。该区域可能构成用于莱姆病更特异和敏感血清学诊断的候选抗原。