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Details on Person Severe acute respiratory syndrome coronavirus type 2 (SARS-C...

Class:IdSummation:9754770
_displayNameSevere acute respiratory syndrome coronavirus type 2 (SARS-C...
_timestamp2022-02-17 05:14:07
created[InstanceEdit:9754778] Shamovsky, Veronica, 2021-10-02
literatureReference[LiteratureReference:9754792] SARS-CoV-2 promote autophagy to suppress type I interferon response
[LiteratureReference:9715434] Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) membrane (M) protein inhibits type I and III interferon production by targeting RIG-I/MDA-5 signaling
[LiteratureReference:9716154] A systemic and molecular study of subcellular localization of SARS-CoV-2 proteins
[LiteratureReference:5679204] Autophagosomes form at ER-mitochondria contact sites
[LiteratureReference:9754790] Mitochondria-Associated ER Membranes - The Origin Site of Autophagy
[LiteratureReference:9754766] Autophagy-competent mitochondrial translation elongation factor TUFM inhibits caspase-8-mediated apoptosis
[LiteratureReference:9754769] The Matrix Protein of Human Parainfluenza Virus Type 3 Induces Mitophagy that Suppresses Interferon Responses
[LiteratureReference:9754783] The mitochondrial proteins NLRX1 and TUFM form a complex that regulates type I interferon and autophagy
modified[InstanceEdit:9755979] Shamovsky, Veronica, 2021-10-12
[InstanceEdit:9765909] Shamovsky, Veronica, 2022-02-17
textSevere acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) membrane (M) protein is a glycosylated structural protein with three transmembrane (TM) domains. SARS-CoV-2 M predominantly localizes to the endoplasmic reticulum (ER) and Golgi and is essential for the assembly of viral particles (Zheng Y et al. 2020; Zhang J. et al. 2020). In addition, M associates with the mitochondrion to promote mitophagy (Hui X et al. 2021). In M-expressing human hepatocellular carcinoma (Huh-7.0) cells, M co-localized and interacted with the mitochondrial translation elongation factor Tu (TUFM). TUFM is thought to recruit M to the mitochondria (Hui X et al. 2021). TUFM has been implicated in mitophagy activation upon viral infections such as vesicular stomatitis virus (Lei Y et al. 2012), human parainfluenza virus type 3 (Ding B et al. 2017) and Kaposi’s sarcoma-associated herpesvirus (Choi CY et al. 2021). TUFM promotes autophagy but downregulates mitochondria-mediated antiviral responses including production of type I and III interferon (IFN) and apoptotic signaling pathway (Ding B et al. 2017; Zheng Y et al. 2020; Hui X et al. 2021; Choi CY et al. 2021). Mitochondria-associated viral M in turn recruits microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B or LC3-II) to induce mitophagy. The SARS-CoV-2 M-mediated induction of mitophagy supports the findings that expression of M suppressed MAVS- and DDX58-mediated production of type I and III IFNs in human embryonic kidney 293T cells (HEK293T cells) induced by Sendai virus (SeV) infection (Zheng Y et al. 2020; Hui X et al. 2021). The inhibitory effect of viral M on the production of IFNs was also observed in human alveolar basal epithelial (A549) cells (Zheng Y et al. 2020). These data suggest that SARS-CoV-2 infection promotes mitophagy to suppress IFNs production.

This Reactome event shows binding of the ER-localized SARS-CoV-2 M protein to mitochondrial TUFM assuming that this interaction occurs at the mitochondria-associated endoplasmic reticulum membrane (MAM), which was shown to regulate autophagosomes formation (Hamasaki M et al. 2013; reviewed in Yang M et al. 2020).

(summation)[BlackBoxEvent:9754763] SARS-CoV-2 M protein binds TUFM [Homo sapiens]
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