Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Novel and Emerging Infectious Diseases, Greifswald-Insel Riems, Germany.
Department of Virology, Institut Pasteur, Antiviral Strategies, Paris, France.
Arch Virol. 2021 Nov;166(11):2999-3012. doi: 10.1007/s00705-021-05159-y. Epub 2021 Aug 13.
The orthohantavirus Puumala virus (PUUV), which is transmitted by bank voles (Clethrionomys glareolus), and other vole-borne hantaviruses contain in their small (S) genome segment two overlapping open reading frames, coding for the nucleocapsid protein and the non-structural protein NSs, a putative type I interferon (IFN-I) antagonist. To investigate the role of NSs of PUUV and other orthohantaviruses, the expression pattern of recombinant NSs constructs and their ability to inhibit human IFN-I promoter activity were investigated. The NSs proteins of PUUV and related cricetid-borne orthohantaviruses showed strong inhibition of IFN-I promoter induction. We identified protein products originating from three and two methionine initiation codons in the NSs ORF of PUUV during transfection and infection, respectively. The three putative start codons are conserved in all PUUV strains analysed. Translation initiation at these start codons influenced the inhibitory activity of the NSs products, with the wild-type (wt) construct expressing two proteins starting at the first and second methionine and showing strong inhibition activity. Analysis of in vitro-generated variants and naturally occurring PUUV NSs proteins indicated that amino acid variation in the NSs protein is well tolerated, suggesting its phenotypic plasticity. The N-terminal 20-amino-acid region of the NSs protein was found to be associated with strong inhibition and to be highly vulnerable to amino acid exchanges and tag fusions. Infection studies using human, bank vole, and Vero E6 cells did not show obvious differences in the replication capacity of PUUV Sotkamo wt and a strain with a truncated NSs protein (NSs21Stop), showing that the lack of a full-length NSs might be compensated by its N-terminal peptide, as seen in transfection experiments. These results contribute to our understanding of virus-host interactions and highlight the importance of future innate immunity studies in reservoir hosts.
沙鼠型汉坦病毒(PUUV)由田鼠(Clethrionomys glareolus)传播,其他由田鼠传播的汉坦病毒在其小(S)基因组片段中包含两个重叠的开放阅读框,编码核衣壳蛋白和非结构蛋白 NSs,这是一种假定的 I 型干扰素(IFN-I)拮抗剂。为了研究 PUUV 和其他正粘病毒的 NSs 的作用,研究了重组 NSs 构建体的表达模式及其抑制人 IFN-I 启动子活性的能力。PUUV 和相关的仓鼠源性正粘病毒的 NSs 蛋白强烈抑制 IFN-I 启动子诱导。我们在转染和感染过程中分别鉴定了来自 PUUV NSs ORF 中的三个和两个甲硫氨酸起始密码子的蛋白产物。所有分析的 PUUV 株都保守了这三个假定的起始密码子。NSs 产物的翻译起始受起始密码子的影响,wt 构建体表达从第一个和第二个甲硫氨酸开始的两个蛋白,具有很强的抑制活性。对体外产生的变体和天然存在的 PUUV NSs 蛋白的分析表明,NSs 蛋白中的氨基酸变异是可以耐受的,表明其表型可塑性。NSs 蛋白的 N 端 20 个氨基酸区域与强烈抑制相关,并且对氨基酸交换和标记融合高度敏感。使用人、田鼠和 Vero E6 细胞进行的感染研究表明,PUUV Sotkamo wt 和具有截断 NSs 蛋白(NSs21Stop)的菌株在复制能力方面没有明显差异,表明缺乏全长 NSs 可能由其 N 端肽补偿,正如转染实验中所见。这些结果有助于我们了解病毒-宿主相互作用,并强调了在宿主动物中进行固有免疫研究的重要性。