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首页> 外文期刊>Virus Genes >Conserved cysteine residues within the attachment G glycoprotein of respiratory syncytial virus play a critical role in the enhancement of cytotoxic T-lymphocyte responses.
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Conserved cysteine residues within the attachment G glycoprotein of respiratory syncytial virus play a critical role in the enhancement of cytotoxic T-lymphocyte responses.

机译：呼吸道合胞病毒附着G糖蛋白内的保守半胱氨酸残基在增强细胞毒性T淋巴细胞反应中起关键作用。

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摘要

The cytotoxic T-lymphocyte (CTL) response plays an important role in the control of respiratory syncytial virus (RSV) replication and the establishment of a Th1-CD4+ T cell response against the virus. Despite lacking Major Histocompatibility Complex I (MHC I)-restricted epitopes, the attachment G glycoprotein of RSV enhances CTL activity toward other RSV antigens, and this effect depends on its conserved central region. Here, we report that RSV-G can also improve CTL activity toward antigens from unrelated pathogens such as influenza, and that a mutant form of RSV-G lacking four conserved cysteine residues at positions 173, 176, 182, and 186 fails to enhance CTL responses. Our results indicate that these conserved residues are essential for the wide-spectrum pro-CTL activity displayed by the protein.
机译：细胞毒性T淋巴细胞（CTL）应答在控制呼吸道合胞病毒（RSV）复制和建立针对该病毒的Th1-CD4 + T细胞应答中起重要作用。尽管缺少主要组织相容性复合物I（MHC I）限制的表位，RSV的附着G糖蛋白仍增强了对其他RSV抗原的CTL活性，这种作用取决于其保守的中心区域。在这里，我们报道RSV-G还可以提高针对不相关病原体（例如流感）的抗原的CTL活性，而突变形式的RSV-G在173、176、182和186位缺少四个保守的半胱氨酸残基不能增强CTL回应。我们的结果表明，这些保守的残基对于蛋白质显示的广谱促CTL活性至关重要。

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