Emmrich F, Bundle D, van der Zee J, Out T, Zenke G, Eichmann K
Scand J Immunol. 1985 Feb;21(2):119-26. doi: 10.1111/j.1365-3083.1985.tb01410.x.
Five hundred and fifty human sera from patients with IgM myeloma or Waldenström's macroglobulinaemia were screened by a solid-phase enzyme-linked immunoassay for binding to the carbohydrate of group A streptococci (A-CHO). Two of them (AC8 and AC179) contained immunoglobulin, which bound specifically to A-CHO even at serum dilutions of 1:10(7). Using synthetic oligosaccharides coupled to protein for inhibition studies, the fine specificities of AC8 and AC179 were determined. AC179 is directed to alpha-linked rhamnose oligosaccharides. AC8 appears to be specific for N-acetyl-D-glucosamine (GlcNAc) side chains beta(1----2)-linked to rhamnose, whereas GlcNAc side chains in A-CHO are reported to be beta(1----3)-linked to the rhamnose backbone. Naturally occurring anti-A-CHO antibodies consist mainly of low-affinity antibodies to such beta(1----3)-linked GlcNAc. In contrast, both myeloma antibodies show more than 10 times higher relative affinities to A-CHO than antibodies prepared from normal human serum (anti-GlcNAc and anti-A-CHO, respectively) by selection for high affinity in the elution procedure. AC179 induced complement activation in the presence of A-CHO.
采用固相酶联免疫分析法，对550份来自IgM骨髓瘤或华氏巨球蛋白血症患者的人血清进行筛查，以检测其与A组链球菌碳水化合物（A-CHO）的结合情况。其中两份血清（AC8和AC179）含有免疫球蛋白，即使在血清稀释至1:10(7)时，仍能特异性结合A-CHO。通过使用与蛋白质偶联的合成寡糖进行抑制研究，确定了AC8和AC179的精细特异性。AC179针对α-连接的鼠李糖寡糖。AC8似乎对与鼠李糖β(1----2)连接的N-乙酰-D-葡萄糖胺（GlcNAc）侧链具有特异性，而据报道A-CHO中的GlcNAc侧链是与鼠李糖主链β(1----3)连接的。天然存在的抗A-CHO抗体主要由针对此类β(1----3)连接的GlcNAc的低亲和力抗体组成。相比之下，这两种骨髓瘤抗体对A-CHO的相对亲和力比通过洗脱过程中选择高亲和力从正常人血清制备的抗体（分别为抗GlcNAc和抗A-CHO）高10倍以上。AC179在存在A-CHO的情况下可诱导补体激活。
