De Bolle X, Laurent T, Tibor A, Godfroid F, Weynants V, Letesson J J, Mertens P
Immunology and Microbiology Laboratory, Research Unit in Molecular Biology (URBM), University of Namur (FUNDP), 61 rue de Bruxelles, Namur, B5000, Belgium.
J Mol Biol. 1999 Nov 19;294(1):181-91. doi: 10.1006/jmbi.1999.3248.
The lipopolysaccharide (LPS) is up to now the only identified major virulence determinant of Brucella. This bacterium is responsible for brucellosis in animals and for Malta fever in humans. Several monoclonal antibodies (mAbs) directed against various LPS epitopes have been characterized. Two mAbs, named A15-6B3 and B66-2C8, directed against distinct LPS epitopes have been used to select peptides from 11 phage display libraries. The sequences of the selected peptides contain an overrepresentation of either proline or tryptophan residues when selected with either A15-6B3 or B66-2C8 mAbs, respectively. For the best binding peptides, competition with LPS for the binding to the mAb is detected, which suggests that the peptides bind to the paratope of the mAb. The phages selected from the libraries were used to immunise mice, and a weak antibody response directed against LPS has been observed. These data suggest that a subset of the selected peptides are mimotopes of the LPS epitopes.
脂多糖(LPS)是目前唯一已确定的布鲁氏菌主要毒力决定因素。这种细菌可导致动物患布鲁氏菌病以及人类患马耳他热。已对多种针对不同LPS表位的单克隆抗体(mAb)进行了特性鉴定。两种分别名为A15 - 6B3和B66 - 2C8、针对不同LPS表位的单克隆抗体已被用于从11个噬菌体展示文库中筛选肽段。当分别用A15 - 6B3或B66 - 2C8单克隆抗体筛选时,所选肽段的序列中脯氨酸或色氨酸残基出现的频率过高。对于结合能力最强的肽段,检测到其与LPS竞争结合单克隆抗体,这表明这些肽段与单克隆抗体的互补决定区结合。从文库中筛选出的噬菌体用于免疫小鼠,观察到针对LPS的微弱抗体反应。这些数据表明,所选肽段中的一部分是LPS表位的模拟表位。