糖基化修饰调节沙粒病毒糖蛋白的表达和功能。
Glycosylation modulates arenavirus glycoprotein expression and function.
机构信息
University of California, Irvine, Department of Molecular Biology and Biochemistry & Division of Infectious Disease, 3205 McGaugh Hall, Irvine, CA 92697-3900, USA.
出版信息
Virology. 2011 Jan 20;409(2):223-33. doi: 10.1016/j.virol.2010.10.011. Epub 2010 Nov 5.
The glycoprotein of lymphocytic choriomeningitis virus (LCMV) contains nine potential N-linked glycosylation sites. We investigated the function of these N-glycosylations by using alanine-scanning mutagenesis. All the available sites were occupied on GP1 and two of three on GP2. N-linked glycan mutations at positions 87 and 97 on GP1 resulted in reduction of expression and absence of cleavage and were necessary for downstream functions, as confirmed by the loss of GP-mediated fusion activity with T87A and S97A mutants. In contrast, T234A and E379N/A381T mutants impaired GP-mediated cell fusion without altered expression or processing. Infectivity via virus-like particles required glycans and a cleaved glycoprotein. Glycosylation at the first site within GP2, not normally utilized by LCMV, exhibited increased VLP infectivity. We also confirmed the role of the N-linked glycan at position 173 in the masking of the neutralizing epitope GP-1D. Taken together, our results indicated a strong relationship between fusion and infectivity.
淋巴细胞性脉络丛脑膜炎病毒（LCMV）的糖蛋白含有九个潜在的 N 连接糖基化位点。我们通过使用丙氨酸扫描诱变研究了这些 N 糖基化的功能。所有可用的位点都在 GP1 上被占据，而在 GP2 上有三个中的两个。在 GP1 上的位置 87 和 97 的 N 连接聚糖突变导致表达减少和缺失切割，并且对于下游功能是必要的，这通过与 T87A 和 S97A 突变体的 GP 介导的融合活性的丧失得到证实。相比之下，T234A 和 E379N/A381T 突变体在不改变表达或加工的情况下损害了 GP 介导的细胞融合。通过病毒样颗粒的感染需要糖基化和切割的糖蛋白。GP2 内第一个位点的糖基化，通常不由 LCMV 使用，表现出增加的 VLPs 感染性。我们还证实了 GP2 中位置 173 的 N 连接聚糖在中和表位 GP-1D 掩蔽中的作用。总之，我们的结果表明融合和感染性之间存在很强的关系。
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