An antibody-based proximity labeling map reveals mechanisms of SARS-CoV-2 inhibition of antiviral immunity

Zhang, Yuehui; Shang, Limin; Zhang, Jing; Liu, Yuchen; Jin, Chaozhi; Zhao, Yanan; Lei, Xiaobo; Wang, Wenjing; Xiao, Xia; Zhang, Xiuyuan; Liu, Yujiao; Liu, Linlin; Zhuang, Meng-Wei; Mi, Qingkun; Tian, Chunyan; Wang, Jianwei; He, Fuchu; Wang, Pei‐Hui; Wang, Jian

doi:10.1016/j.chembiol.2021.10.008

Cited by 29 publications

(32 citation statements)

References 65 publications

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“…Although not significantly enriched in our datasets, two other previously documented interaction partners of SARS-CoV-2 Spike, namely ITGB1 and Vimentin (VIM), were detected across all modalities in agreement with previous IP-MS and immunostaining reports (Amraei et al, 2022; Suprewicz et al, 2021; Zhang et al, 2022). However, VIM has also been reported as a common contaminant by LC-MS/MS (Mellacheruvu et al, 2013).…”

Section: Resultssupporting

confidence: 91%

“…The identification of these interacting host factors may explain the susceptibility of diverse human cells and tissues exhibiting low to undetectable ACE2 levels to SARS-CoV-2 infection (Chen et al ., 2021; Li et al ., 2020). The number of host factors in spatial proximity with the viral Spike protein also proves its promiscuous binding nature and motivates future studies aimed at uncovering their respective binding pockets on the trimeric Spike protein complex, as was recently documented for the NRP1, ganglioside and integrin-binding motifs on Spike (Lempp et al ., 2021; Zhang et al ., 2022).…”

Section: Discussionmentioning

confidence: 99%

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High resolution photocatalytic mapping of SARS-CoV-2 Spike protein-host cell membrane interactions

Datta

Tavares

Reyes‐Robles

et al. 2022

Preprint

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Identifying protein environments at the virus-host cell interface can improve our understanding of viral entry and pathogenesis. SARS-CoV-2, the virus behind the ongoing COVID-19 pandemic, uses the cell surface ACE2 protein as a major receptor, but the contribution of other cellular proteins in the entry process is unknown. To probe the microenvironment of SARS-CoV-2 Spike-ACE2 protein interactomes on human cells, we developed a photocatalyst-based viral-host protein microenvironment mapping platform (ViraMap) employing iridium photocatalysts conjugated to Spike for visible-light driven proximity labelling on host cells. Application of ViraMap on ACE2-expressing cells captured ACE2, the established co-receptor NRP1, as well as other proteins implicated in host cell entry and immunomodulation. We further investigated these enriched proteins via loss-of-function and over-expression in pseudotype and authentic infection models and observed that the Ig receptor PTGFRN and tyrosine kinase ligand EFNB1 can serve as SARS-CoV-2 entry factors. Our results highlight additional host targets that participate infection and showcase ViraMap for interrogating virus-host cell surface interactomes.

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Section: Resultssupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

High resolution photocatalytic mapping of SARS-CoV-2 Spike protein-host cell membrane interactions

Datta

Tavares

Reyes‐Robles

et al. 2022

Preprint

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“…We have constructed the plasmids that can well express 29 SARS‐CoV‐2‐encoded viral proteins in our previous studies. 18 , 27 To screen which of these viral proteins may play a role in dampening the STING signaling, we transfected the STING expression vector together with plasmids expressing empty vector (control) or individual SARS‐CoV‐2 proteins into HEK293T cells. Thirty‐six hours later, the cells were harvested for the detection of IFN‐β mRNA expression using RT‐qPCR.…”

Section: Resultsmentioning

confidence: 99%

“…Plasmids expressing cGAS, STING, TBK1, or various SARA‐CoV‐2 proteins were constructed in our previous publications. 15 , 16 , 17 , 18 IFN‐β luciferase reporter plasmid pGL3‐IFN‐β‐Luc, IFN‐λ1 luciferase reporter plasmid pGL3‐IFN‐λ1‐Luc, and ISG luciferase reporter plasmid pISRE‐Luc have been described previously. 19 , 20 , 21 SARS‐CoV‐2 ORF10 gene (Gene ID: 43740576) was synthesized according to the genome sequence of the SARA‐CoV‐2 Wuhan‐Hu‐1 strain (NC_045512.2) (GENERAL BIOL) and cloned into pCAG expression vector.…”

Section: Methodsmentioning

confidence: 99%

SARS‐CoV‐2 ORF10 antagonizes STING‐dependent interferon activation and autophagy

Han

Zheng

Deng

et al. 2022

Journal of Medical Virology

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A characteristic feature of COVID‐19, the disease caused by severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) infection, is the dysregulated immune response with impaired type I and III interferon (IFN) expression and an overwhelming inflammatory cytokine storm. RIG‐I‐like receptors (RLRs) and cGAS–STING signaling pathways are responsible for sensing viral infection and inducing IFN production to combat invading viruses. Multiple proteins of SARS‐CoV‐2 have been reported to modulate the RLR signaling pathways to achieve immune evasion. Although SARS‐CoV‐2 infection also activates the cGAS–STING signaling by stimulating micronuclei formation during the process of syncytia, whether SARS‐CoV‐2 modulates the cGAS–STING pathway requires further investigation. Here, we screened 29 SARS‐CoV‐2‐encoded viral proteins to explore the viral proteins that affect the cGAS–STING signaling pathway and found that SARS‐CoV‐2 open reading frame 10 (ORF10) targets STING to antagonize IFN activation. Overexpression of ORF10 inhibits cGAS–STING‐induced interferon regulatory factor 3 phosphorylation, translocation, and subsequent IFN induction. Mechanistically, ORF10 interacts with STING, attenuates the STING–TBK1 association, and impairs STING oligomerization and aggregation and STING‐mediated autophagy; ORF10 also prevents the endoplasmic reticulum (ER)‐to‐Golgi trafficking of STING by anchoring STING in the ER. Taken together, these findings suggest that SARS‐CoV‐2 ORF10 impairs the cGAS–STING signaling by blocking the translocation of STING and the interaction between STING and TBK1 to antagonize innate antiviral immunity.

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“…Meanwhile, SARS-CoV-2 use various strategies to antagonize the host antiviral response allowing the virus to replicate robustly after entering the cell ( 152 – 156 ). The accessory proteins ORF3b, ORF6, ORF7a and ORF7b antagonize the production and signal transmission of IFN-I, while ORF8 disrupts antigen presentation by downregulating major histocompatibility complex class I (MHC-I) ( 133 , 153 , 157 , 158 ). In order to block the interferon receptor signal transmission, ORF7a interrupts STAT2 phosphorylation and inhibits the activation of antiviral ISGs ( 152 , 155 , 159 – 161 ).…”

Section: Sars-cov-2 Suppresses Host Protein Translationmentioning

confidence: 99%

Translational Control of COVID-19 and Its Therapeutic Implication

et al. 2022

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The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of COVID-19, which has broken out worldwide for more than two years. However, due to limited treatment, new cases of infection are still rising. Therefore, there is an urgent need to understand the basic molecular biology of SARS-CoV-2 to control this virus. SARS-CoV-2 replication and spread depend on the recruitment of host ribosomes to translate viral messenger RNA (mRNA). To ensure the translation of their own mRNAs, the SARS-CoV-2 has developed multiple strategies to globally inhibit the translation of host mRNAs and block the cellular innate immune response. This review provides a comprehensive picture of recent advancements in our understanding of the molecular basis and complexity of SARS-CoV-2 protein translation. Specifically, we summarize how this viral infection inhibits host mRNA translation to better utilize translation elements for translation of its own mRNA. Finally, we discuss the potential of translational components as targets for therapeutic interventions.

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An antibody-based proximity labeling map reveals mechanisms of SARS-CoV-2 inhibition of antiviral immunity

Cited by 29 publications

References 65 publications

High resolution photocatalytic mapping of SARS-CoV-2 Spike protein-host cell membrane interactions

High resolution photocatalytic mapping of SARS-CoV-2 Spike protein-host cell membrane interactions

SARS‐CoV‐2 ORF10 antagonizes STING‐dependent interferon activation and autophagy

Translational Control of COVID-19 and Its Therapeutic Implication

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