Makino S, Yamamoto K, Murakami S, Shirahata T, Uemura K, Sawada T, Wakamoto H, Morita H
Department of Veterinary Microbiology, University of Agriculture and Veterinary Medicine, Hokkaido, Obihiro, 080-8555, Japan.
Microb Pathog. 1998 Aug;25(2):101-9. doi: 10.1006/mpat.1998.0216.
Erysipelothrix rhusiopathiae is a small gram-positive rod bacterium that causes erysipelas in swine and a variety of diseases in other animals and humans. Although live-attenuated or bacterin vaccines are effective in protecting against erysipelas, the genetic construction of their active antigen has not been identified. To clarify the surface antigen(s) involved in protective and arthritic response, using monoclonal antibody I2A against the surface proteins of E. rhusiopathiae, we identified a protective antigen, which consists of 606 amino acids. Analysis of deletion derivatives of the gene, spaA(surface protective antigen), showed that the SpaA protein binds tightly to the bacterial cell surface via eight repeat units with a GW-module consisting of 20 amino acids at the C-terminus. Although DeltaSpaA lacking their repeat units lost its ability to induce protection against E. rhusiopathiae infection, intact SpaA protein showed the protection. We conclude that the presence of repeat units is essential both for the binding of SpaA to the bacterial cell surface and for protection. We believe that the repeat region at the C-terminus should be a candidate for a subunit vaccine against erysipelas.
猪红斑丹毒丝菌是一种革兰氏阳性小杆菌，可引起猪的丹毒以及其他动物和人类的多种疾病。尽管减毒活疫苗或菌苗在预防丹毒方面有效，但其活性抗原的基因结构尚未明确。为了阐明参与保护性和关节炎反应的表面抗原，我们使用抗猪红斑丹毒丝菌表面蛋白的单克隆抗体I2A，鉴定出一种由606个氨基酸组成的保护性抗原。对表面保护性抗原基因spaA的缺失衍生物进行分析表明，SpaA蛋白通过八个重复单元与细菌细胞表面紧密结合，其C末端有一个由20个氨基酸组成的GW模块。虽然缺少重复单元的DeltaSpaA失去了诱导抵抗猪红斑丹毒丝菌感染的保护能力，但完整的SpaA蛋白具有保护作用。我们得出结论，重复单元的存在对于SpaA与细菌细胞表面的结合以及保护作用都至关重要。我们认为C末端的重复区域应是抗丹毒亚单位疫苗的一个候选区域。
