Group a streptococcal antigens cross-reactive with myocardium. Purification of heart-reactive antibody and isolation and characterization of the streptococcal antigen
Group a streptococcal antigens cross-reactive with myocardium. Purification of heart-reactive antibody and isolation and characterization of the streptococcal antigen
复制标题
A组链球菌抗原与心肌发生交叉反应。
DOI：
--
复制
发表时间：
1977
影响因子：
15.3
通讯作者：
M. Mccarty
中科院分区：
文献类型：
--
作者：
I. V. D. Rijn;JB Sabriskie;M. Mccarty
实验动物接种A群链球菌后，血清中出现心脏反应性抗体（HRA），急性风湿热病人也出现HRA。用A组链球菌膜吸附任一血清将去除HRA。这两种类型的HRA之间的阻断实验已经证明，抗体针对相同或不同分子上的不同抗原决定簇。从风湿热病人血清中分离纯化HRA，是从与心肌纤维肌膜鞘交叉反应的A组链球菌中分离纯化抗原的必要条件。将含有所有HRA的分离的γ球蛋白吸附到人肌膜鞘上。使用碘化钾释放特定的HRA。超过99%的纯化的HRA被证明与肌膜鞘结合，而不到1%的抗体与其他物质非特异性结合。A组链球菌膜的制备物将以97%或更高的水平结合从急性风湿病患者血清中纯化的HRA。用非离子去污剂增溶的交叉反应性抗原通过柱层析纯化120倍。在十二烷基硫酸钠聚丙烯酰胺电泳上，证明该抗原由四种多肽组成，分子量分别为32，000、28，000、26，000和22，000道尔顿。只有蛋白水解酶可以破坏抗原决定簇，而糖苷酶和脂肪酶没有效果。纯化的抗原阻断了纯化的HRA与正常人心脏切片的结合。
Heart-reactive antibody (HRA) appears in the sera of experimental animals inoculated with group A streptococci as well as patients with acute rheumatic fever. Adsorption of either serum with group A streptococcal membranes will remove the HRA. Blocking experiments between these two types of HRAs have demonstrated that the antibodies are directed towards different antigenic determinants on either the same or different molecules. To isolate and purify the antigen from the group A streptococcus cross-reactive with sarcolemmal sheaths of cardiac myofibers, it became necessary to purify the HRA from rheumatic fever patients’ sera. Isolated gamma globulin containing all of the HRA was adsorbed onto human sarcolemmal sheaths. The specific HRA was released by using potassium iodide. Over 99 percent of the purified HRA was shown to bind the sarcolemmal sheath whereas less than 1 percent of the antibody would bind nonspecifically to other material. Preparations of group A streptococcal membrane will bind HRA purified from the sera of acute rheumatic patients at levels of 97 percent or greater. The cross-reactive antigen solubilized by nonionic detergent was purified 120-fold by column chromatography. On sodium dodecyl sulfate polyacrylamide electrophoresis, the antigen was demonstrated to be composed of four polypeptides with mol wt of 32,000, 28,000, 26,000, and 22,000 daltons, respectively. Only proteolytic enzymes could destroy the antigenic determinant whereas glycosidases and lipases had no effect. The purified antigen blocked the binding of purified HRA to normal human heart sections.