Top F H, Wannamaker L W
J Exp Med. 1968 May 1;127(5):1013-34. doi: 10.1084/jem.127.5.1013.
Investigation into the antigenicity of streptococcal lipoproteinase has revealed the existence of multiple, immunologically distinct enzymes. Each lipoproteinase identified was found to be strain specific in that it was found only in strains of a particular T-agglutination pattern. In some T patterns, all streptococci of that T pattern which were examined shared a common lipoproteinase antigen. In other T patterns, strains which produced antigenically different lipoproteinases were identified. Evidence that the lipoproteinase antigen is distinct from other well-established cellular antigens of Group A streptococci has been presented. The production of this strain-specific enzyme by strains currently difficult to type by the standard M precipitin method may facilitate more precise identification of these strains and a better assessment of their role in the pathogenesis of Group A streptococcal infections and their sequelae.
对链球菌脂蛋白酶抗原性的研究揭示了多种免疫上不同的酶的存在。所鉴定的每种脂蛋白酶都具有菌株特异性,因为它仅在具有特定T凝集模式的菌株中发现。在某些T模式中,所检测的该T模式的所有链球菌都共享一种共同的脂蛋白酶抗原。在其他T模式中,鉴定出产生抗原性不同的脂蛋白酶的菌株。已提出证据表明脂蛋白酶抗原与A组链球菌其他已明确的细胞抗原不同。目前难以通过标准M沉淀素方法分型的菌株产生这种菌株特异性酶,可能有助于更精确地鉴定这些菌株,并更好地评估它们在A组链球菌感染及其后遗症发病机制中的作用。