Division of Veterinary Medicine, Paul-Ehrlich-Institut, 63225 Langen, Germany.
European Virus Bioinformatics Center, 07743 Jena, Germany.
Proc Natl Acad Sci U S A. 2024 Jun 4;121(23):e2407437121. doi: 10.1073/pnas.2407437121. Epub 2024 May 30.
The accessory protease transmembrane protease serine 2 (TMPRSS2) enhances severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) uptake into ACE2-expressing cells, although how increased entry impacts downstream viral and host processes remains unclear. To investigate this in more detail, we performed infection assays in engineered cells promoting ACE2-mediated entry with and without TMPRSS2 coexpression. Electron microscopy and inhibitor experiments indicated TMPRSS2-mediated cell entry was associated with increased virion internalization into endosomes, and partially dependent upon clathrin-mediated endocytosis. TMPRSS2 increased panvariant uptake efficiency and enhanced early rates of virus replication, transcription, and secretion, with variant-specific profiles observed. On the host side, transcriptional profiling confirmed the magnitude of infection-induced antiviral and proinflammatory responses were linked to uptake efficiency, with TMPRSS2-assisted entry boosting early antiviral responses. In addition, TMPRSS2-enhanced infections increased rates of cytopathology, apoptosis, and necrosis and modulated virus secretion kinetics in a variant-specific manner. On the virus side, convergent signatures of cell-uptake-dependent innate immune induction were recorded in viral genomes, manifesting as switches in dominant coupled Nsp3 residues whose frequencies were correlated to the magnitude of the cellular response to infection. Experimentally, we demonstrated that selected Nsp3 mutations conferred enhanced interferon antagonism. More broadly, we show that TMPRSS2 orthologues from evolutionarily diverse mammals facilitate panvariant enhancement of cell uptake. In summary, our study uncovers previously unreported associations, linking cell entry efficiency to innate immune activation kinetics, cell death rates, virus secretion dynamics, and convergent selection of viral mutations. These data expand our understanding of TMPRSS2's role in the SARS-CoV-2 life cycle and confirm its broader significance in zoonotic reservoirs and animal models.
辅助蛋白酶跨膜丝氨酸蛋白酶 2(TMPRSS2)增强严重急性呼吸综合征冠状病毒 2(SARS-CoV-2)进入 ACE2 表达细胞的能力,尽管增加的进入如何影响下游病毒和宿主过程尚不清楚。为了更详细地研究这一点,我们在促进 ACE2 介导进入的工程细胞中进行了感染实验,同时有无 TMPRSS2 共表达。电子显微镜和抑制剂实验表明,TMPRSS2 介导的细胞进入与病毒进入内体的内化增加有关,部分依赖于网格蛋白介导的内吞作用。TMPRSS2 增加了 panvariant 的摄取效率,并增强了病毒复制、转录和分泌的早期速率,观察到变体特异性谱。在宿主方面,转录谱分析证实感染诱导的抗病毒和促炎反应的程度与摄取效率有关,TMPRSS2 辅助进入增强了早期抗病毒反应。此外,TMPRSS2 增强的感染增加了细胞病变、细胞凋亡和坏死的速率,并以变体特异性的方式调节病毒分泌动力学。在病毒方面,记录到与细胞摄取依赖性先天免疫诱导相关的收敛特征在病毒基因组中,表现为主导耦合 Nsp3 残基的转变,其频率与感染后细胞对感染的反应幅度相关。实验上,我们证明了选定的 Nsp3 突变赋予了增强的干扰素拮抗作用。更广泛地说,我们表明,来自进化上不同的哺乳动物的 TMPRSS2 同源物促进了 panvariant 增强的细胞摄取。总之,我们的研究揭示了以前未报告的关联,将细胞进入效率与先天免疫激活动力学、细胞死亡率、病毒分泌动力学和病毒突变的收敛选择联系起来。这些数据扩展了我们对 TMPRSS2 在 SARS-CoV-2 生命周期中的作用的理解,并证实了它在人畜共患病宿主和动物模型中的更广泛意义。