de Vries N, Zwaagstra K A, Huis in't Veld J H, van Knapen F, van Zijderveld F G, Kusters J G
Department of the Science of Food of Animal Origin, The Netherlands.
Appl Environ Microbiol. 1998 Dec;64(12):5033-8. doi: 10.1128/AEM.64.12.5033-5038.1998.
Salmonella typhimurium expresses two antigenically distinct flagellins, each containing a different H antigen (i and 1,2), the combination of which is highly specific for this serotype. In this study, overlapping recombinant flagellin fragments were constructed from the fliC (H:i) and fljB (H:1,2) flagellin genes, and the expression products were tested for binding to H antigen-specific monoclonal and polyclonal antibodies. A minimal area, 86 amino acids for H:i and 102 amino acids for H:1,2, located in the central variable domain of each flagellin was required for the binding of serotype-specific antibodies, providing further evidence for the presence of a discontinuous H epitope. Two peptides comprising these areas were shown to be highly suitable for application as antigens in an enzyme-linked immunosorbent assay detecting S. typhimurium-specific antibody.
鼠伤寒沙门氏菌表达两种抗原性不同的鞭毛蛋白,每种都含有不同的H抗原(i和1,2),其组合对该血清型具有高度特异性。在本研究中,从fliC(H:i)和fljB(H:1,2)鞭毛蛋白基因构建了重叠的重组鞭毛蛋白片段,并测试了表达产物与H抗原特异性单克隆和多克隆抗体的结合情况。血清型特异性抗体的结合需要位于每种鞭毛蛋白中央可变域的一个最小区域,H:i为86个氨基酸,H:1,2为102个氨基酸,这为不连续H表位的存在提供了进一步证据。包含这些区域的两种肽被证明非常适合用作酶联免疫吸附测定中检测鼠伤寒沙门氏菌特异性抗体的抗原。