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A群链球菌细胞外半胱氨酸蛋白酶重组突变蛋白的表达与特性分析以及人类侵袭性疾病发作期间血清转化的记录

Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes.

作者信息

Gubba S, Low D E, Musser J M

机构信息

Institute for the Study of Human Bacterial Pathogenesis, Department of Pathology, Baylor College of Medicine, Houston, Texas 77030, USA.

出版信息

Infect Immun. 1998 Feb;66(2):765-70. doi: 10.1128/IAI.66.2.765-770.1998.

Abstract

A recent study with isogenic strains constructed by recombinant DNA strategies unambiguously documented that a highly conserved extracellular cysteine protease expressed by Streptococcus pyogenes (group A Streptococcus [GAS]) is a critical virulence factor in a mouse model of invasive disease (S. Lukomski, S. Sreevatsan, C. Amberg, W. Reichardt, M. Woischnik, A. Podbielski, and J. M. Musser, J. Clin. Invest. 99:2574-2580, 1997). To facilitate further investigations of the streptococcal cysteine protease, recombinant proteins composed of a 40-kDa zymogen containing a C192S amino acid substitution that ablates enzymatic activity, a 28-kDa mature protein with the C192S replacement, and a 12-kDa propeptide were purified from Escherichia coli containing His tag expression vectors. The recombinant C192S zymogen retained apparently normal structural integrity, as assessed by the ability of purified wild-type streptococcal cysteine protease to process the 40-kDa molecule to the 28-kDa mature form. All three recombinant purified proteins retained immunologic reactivity with polyclonal and monoclonal antibodies. Humans with a diverse range of invasive disease episodes (erysipelas, cellulitis, pneumonia, bacteremia, septic arthritis, streptococcal toxic shock syndrome, and necrotizing fasciitis) caused by six distinct M types of GAS seroconverted to the streptococcal cysteine protease. These results demonstrate that this GAS protein is expressed in vivo during the course of human infections and thereby provide additional evidence that the cysteine protease participates in host-pathogen interactions in some patients.

摘要

最近一项利用重组DNA策略构建同基因菌株的研究明确证明,化脓性链球菌(A组链球菌[GAS])表达的一种高度保守的细胞外半胱氨酸蛋白酶是侵袭性疾病小鼠模型中的关键毒力因子(S.卢科姆斯基、S.斯里瓦桑、C.安贝格、W.赖夏德特、M.沃伊施尼克、A.波德别尔斯基和J.M.穆塞尔,《临床研究杂志》99:2574 - 2580,1997年)。为便于进一步研究链球菌半胱氨酸蛋白酶,从含有His标签表达载体的大肠杆菌中纯化了由含有C192S氨基酸取代(消除酶活性)的40 kDa酶原、具有C192S取代的28 kDa成熟蛋白和12 kDa前肽组成的重组蛋白。通过纯化的野生型链球菌半胱氨酸蛋白酶将40 kDa分子加工成28 kDa成熟形式的能力评估,重组C192S酶原显然保留了正常的结构完整性。所有三种重组纯化蛋白都保留了与多克隆和单克隆抗体的免疫反应性。由六种不同M型GAS引起的各种侵袭性疾病发作(丹毒、蜂窝织炎、肺炎、菌血症、化脓性关节炎、链球菌中毒性休克综合征和坏死性筋膜炎)的人类对链球菌半胱氨酸蛋白酶发生了血清转化。这些结果表明,这种GAS蛋白在人类感染过程中在体内表达,从而提供了额外证据,证明半胱氨酸蛋白酶在一些患者中参与宿主 - 病原体相互作用。

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