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首页> 外文期刊>Journal of bacteriology >Identification and Characterization of Two Temperature-Induced Surface-Associated Proteins of Streptococcus suis with High Homologies to Members of the Arginine Deiminase System of Streptococcus pyogenes
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Identification and Characterization of Two Temperature-Induced Surface-Associated Proteins of Streptococcus suis with High Homologies to Members of the Arginine Deiminase System of Streptococcus pyogenes

机译：猪链球菌精氨酸脱氨酶系统成员具有高度同源性的两种温度诱导的猪链球菌表面相关蛋白的鉴定和表征

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The present study was performed to identify stress-induced putative virulence proteins of Streptococcus suis. For this, protein expression patterns of streptococci grown at 32, 37, and 42°C were compared by one- and two-dimensional gel electrophoresis. Temperature shifts from 32 and 37 to 42°C induced expression of two cell wall-associated proteins with apparent molecular masses of approximately 47 and 53 kDa. Amino-terminal sequence analysis of the two proteins indicated homologies of the 47-kDa protein with an ornithine carbamoyltransferase (OCT) from Streptococcus pyogenes and of the 53-kDa protein with the streptococcal acid glycoprotein (SAGP) from S. pyogenes, an arginine deiminase (AD) recently proposed as a putative virulence factor. Cloning and sequencing the genes encoding the putative OCT and AD of S. suis, octS and adiS, respectively, revealed that they had 81.2 (octS) and 80.2% (adiS) identity with the respective genes of S. pyogenes. Both genes belong to the AD system, also found in other bacteria. Southern hybridization analysis demonstrated the presence of the adiS gene in all 42 serotype 2 and 9 S. suis strains tested. In 9 of these 42 strains, selected randomly, we confirmed expression of the AdiS protein, homologous to SAGP, by immunoblot analysis using a specific antiserum against the SAGP of S. pyogenes. In all strains AD activity was detected. Furthermore, by immunoelectron microscopy using the anti-S. pyogenes SAGP antiserum we were able to demonstrate that the AdiS protein is expressed on the streptococcal surface in association with the capsular polysaccharides but is not coexpressed with them.
机译：本研究旨在鉴定应激诱导的猪链球菌毒力蛋白。为此，通过一维和二维凝胶电泳比较在32、37和42℃下生长的链球菌的蛋白表达模式。温度从32和37转变为42°C诱导了两种细胞壁相关蛋白的表达，其表观分子量约为47和53 kDa。两种蛋白质的氨基末端序列分析表明，来自化脓性链球菌的鸟氨酸氨基甲酰基转移酶（OCT）的47 kDa蛋白与来自化脓性链球菌的糖蛋白的53 kDa蛋白的同源性。 S。化脓，一种精氨酸脱亚氨酶（AD），最近被认为是一种潜在的致病因子。对 S的假定OCT和AD编码的基因进行克隆和测序。 suis ， octS 和 adiS 分别显示它们分别为81.2（ octS ）和80.2％（ adiS < / em>）与 S的各个基因的同一性。化脓。这两个基因都属于AD系统，也存在于其他细菌中。 Southern杂交分析表明，在所有42种血清型2和9种 S中均存在 adiS 基因。 suis 菌株。在这42个菌株中，有9个是随机选择的，我们通过使用针对 S的SAGP的特异性抗血清的免疫印迹分析证实了与SAGP同源的AdiS蛋白的表达。化脓。在所有菌株中均检测到AD活性。此外，通过使用抗-S的免疫电子显微镜检查。化脓性SAGP抗血清，我们能够证明AdiS蛋白在链球菌表面与荚膜多糖结合表达，但并未与它们共表达。

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