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首页> 外文期刊>Journal of bacteriology >Four Proteins Encoded in the gspB-secY2A2 Operon of Streptococcus gordonii Mediate the Intracellular Glycosylation of the Platelet-Binding Protein GspB
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Four Proteins Encoded in the gspB-secY2A2 Operon of Streptococcus gordonii Mediate the Intracellular Glycosylation of the Platelet-Binding Protein GspB

机译：戈登链球菌gspB-secY2A2操纵子中编码的四种蛋白质介导血小板结合蛋白GspB的细胞内糖基化。

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Platelet binding by Streptococcus gordonii strain M99 is mediated predominantly by the cell surface glycoprotein GspB. This adhesin consists of a putative N-terminal signal peptide, two serine-rich regions (SRR1 and SRR2), a basic region between SRR1 and SRR2, and a C-terminal cell wall anchoring domain. The glycosylation of GspB is mediated at least in part by Gly and Nss, which are encoded in the secY2A2 locus immediately downstream of gspB. This region also encodes two proteins (Gtf and Orf4) that are required for the expression of GspB but whose functions have not been delineated. In this study, we further characterized the roles of Gly, Nss, Gtf, and Orf4 by investigating the expression and glycosylation of a series of glutathione S-transferase-GspB fusion proteins in M99 and in gly, nss, gtf, and orf4 mutants. Compared with fusion proteins expressed in the wild-type background, fusion proteins expressed in the mutant strain backgrounds showed altered electrophoretic mobility. In addition, the fusion proteins formed insoluble aggregates in protoplasts of the gtf and orf4 mutants. Glycan detection and lectin blot analysis revealed that SRR1 and SRR2 were glycosylated but that the basic region was unmodified. When the fusion protein was expressed in Escherichia coli, glycosylation of this protein was observed only in the presence of both gtf and orf4. These results demonstrate that Gly, Nss, Gtf, and Orf4 are all involved in the intracellular glycosylation of SRRs. Moreover, Gtf and Orf4 are essential for glycosylation, which in turn is important for the solubility of GspB.
机译：戈登链球菌M99菌株的血小板结合主要由细胞表面糖蛋白GspB介导。该粘附素由一个假定的N端信号肽，两个富含丝氨酸的区域（SRR1和SRR2），一个位于SRR1和SRR2之间的碱性区域以及一个C端细胞壁锚定域组成。 GspB的糖基化至少部分由Gly和Nss介导，它们在紧接 gspB 的 secY2A2 位点编码。该区域还编码表达GspB所需的两个蛋白质（Gtf和Orf4），但其功能尚未阐明。在这项研究中，我们通过研究M99和中一​​系列谷胱甘肽 S -转移酶-GspB融合蛋白的表达和糖基化，进一步表征了Gly，Nss，Gtf和Orf4的作用。 gly ， nss ， gtf 和 orf4 突变体。与在野生型背景中表达的融合蛋白相比，在突变菌株背景中表达的融合蛋白显示出改变的电泳迁移率。此外，融合蛋白在 gtf 和 orf4 突变体的原生质体中形成不溶性聚集体。聚糖检测和凝集素印迹分析显示SRR1和SRR2被糖基化，但基本区域未修饰。当融合蛋白在大肠杆菌中表达时，仅在 gtf 和 orf4 同时存在时才观察到该蛋白的糖基化。这些结果表明，Gly，Nss，Gtf和Orf4均参与SRR的细胞内糖基化。此外，Gtf和Orf4对于糖基化至关重要，而糖基化又对GspB的溶解度很重要。

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