Wagner B, Wagner M, Reissbrodt R, Seltmann G
Zentralbl Bakteriol Orig A. 1978 Jun;240(4):517-24.
In studies on the antigenic structure of shigellae, an anodically-moving thermolabile antigen (ATA) was found, which furthermore could be detected in many other enterobacteriae (9, 10). ATA is a glycoprotein with a high molecular heterogeneity, resulting from aggregates of a subunit with a molecular weight of about 22000 Daltons. In the present paper the antigen was localized on the cell surface of several species by means of the immunoferritin technique. Antibodies against the purified ATA were raised in rabbits and were coupled with ferritin using glutaraldehyde. The antigen was found focally distributed over the whole circumference of the cell. According to the location of the ferritin granules, the ATA is tightly attached to the outer membrane. Especially some rough forms of the bacteria were heavily labelled on their surface. From the results obtained we conclude that in the smooth form the polysaccharide side chains of the somatic antigen cover the ATA.
在对志贺氏菌抗原结构的研究中,发现了一种向阳极移动的热不稳定抗原(ATA),此外,在许多其他肠杆菌中也能检测到这种抗原(9,10)。ATA是一种糖蛋白,具有高分子异质性,由分子量约为22000道尔顿的亚基聚集体产生。在本文中,通过免疫铁蛋白技术将该抗原定位在几种细菌的细胞表面。用纯化的ATA免疫兔子制备抗体,并用戊二醛将抗体与铁蛋白偶联。发现抗原集中分布在细胞的整个周边。根据铁蛋白颗粒的位置,ATA紧密附着在外膜上。特别是一些粗糙型细菌的表面被大量标记。从获得的结果我们得出结论,在光滑型细菌中,菌体抗原的多糖侧链覆盖了ATA。