对来自含有emm12和emm55基因的化脓性链球菌菌株的一种补体结合蛋白DRS的特性分析。
Characterization of a complement-binding protein, DRS, from strains of Streptococcus pyogenes containing the emm12 and emm55 genes.
作者信息
Binks Michael, Sriprakash K S
机构信息
Queensland Institute of Medical Research, 300 Herston Road, Herston, Queensland 4006, Australia.
出版信息
Infect Immun. 2004 Jul;72(7):3981-6. doi: 10.1128/IAI.72.7.3981-3986.2004.
Abstract
An extracellular protein of Streptococcus pyogenes, streptococcal inhibitor of complement (SIC), and its variant, called DRS (distantly related to SIC), are expressed by some S. pyogenes strains. SIC from type 1 (M1) isolates of S. pyogenes interferes with complement-mediated cell lysis, reportedly via its interaction with complement proteins. In this study we demonstrate that S. pyogenes strains carrying emm12 and emm55 (the genes for the M12 and M55 proteins, respectively) express and secrete DRS. This protein, like SIC, binds to the C6 and C7 complement proteins, and competition enzyme-linked immunosorbent assay experiments demonstrate that DRS competes with SIC for C6 and C7 binding. Similarly, SIC competes with DRS for binding to the complement proteins. Despite this, the recombinant DRS preparation showed no significant effect on complement function, as determined by lysis of sensitized sheep erythrocytes. Furthermore, the presence of DRS is not inhibitory to SIC activity.
摘要
化脓性链球菌的一种细胞外蛋白——补体链球菌抑制剂（SIC）及其变体DRS（与SIC远缘相关），由一些化脓性链球菌菌株表达。来自化脓性链球菌1型（M1）分离株的SIC据报道通过与补体蛋白相互作用来干扰补体介导的细胞裂解。在本研究中，我们证明携带emm12和emm55（分别为M12和M55蛋白的基因）的化脓性链球菌菌株表达并分泌DRS。该蛋白与SIC一样，可结合C6和C7补体蛋白，竞争酶联免疫吸附测定实验表明DRS与SIC竞争C6和C7的结合。同样，SIC也与DRS竞争结合补体蛋白。尽管如此，通过致敏绵羊红细胞裂解测定，重组DRS制剂对补体功能无显著影响。此外，DRS的存在对SIC活性无抑制作用。
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