Conserved cysteine residues within the attachment G glycoprotein of respiratory syncytial virus play a critical role in the enhancement of cytotoxic T-lymphocyte responses.
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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DOI：
10.1007/s11262-010-0545-9
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发表时间：
2011-02
期刊：
影响因子：
1.6
通讯作者：
Irusta PM
中科院分区：
文献类型：
--
作者：
Melendi GA;Bridget D;Monsalvo AC;Laham FF;Acosta P;Delgado MF;Polack FP;Irusta PM
细胞毒性 T 淋巴细胞 (CTL) 反应在控制呼吸道合胞病毒 (RSV) 复制和建立针对病毒的 Th1-CD4+ T 细胞反应中发挥着重要作用。尽管缺乏主要组织相容性复合物 I (MHC I) 限制性表位，RSV 的附着 G 糖蛋白增强了针对其他 RSV 抗原的 CTL 活性，并且这种作用取决于其保守的中心区域。在这里，我们报告RSV-G还可以提高针对来自无关病原体（例如流感）的抗原的CTL活性，并且在位置173、176、182和186处缺乏四个保守半胱氨酸残基的RSV-G突变体形式无法增强CTL反应。我们的结果表明，这些保守残基对于该蛋白质表现出的广谱 pro-CTL 活性至关重要。
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.