ArticleScientific reports2026
NEAT1 drives SARS-CoV-2 N protein-induced inflammation, metabolic reprogramming, and mitochondria-ER stress crosstalk.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- N6-methyladenosine as a potential epitranscriptomic immune rheostat during SARS-CoV-2 infection.Frontiers in immunology · 2026Review
- Mitochondria-associated membranes in heart failure: from molecular mechanisms to therapeutic targets.Frontiers in physiology · 2026Review
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Authors and funding
12 authors.
Funding
Abstract
SARS-CoV-2 remains a global health concern. Although its nucleocapsid (N) protein supports viral replication and evades host immunity, its role in host metabolic reprogramming and organelle homeostasis is not fully understood. This study aims to elucidate whether the N protein modulates glycolysis and mitochondrial-ER stress crosstalk via the long non-coding RNA NEAT1. We established human bronchial epithelial (HBE) cells stably expressing the N protein. Inflammatory and glycolytic gene expression was analyzed by qRT-PCR and Western blot. ROS levels were measured by flow cytometry, while mitochondrial membrane potential, Ca²⁺ overload, and mitochondria-ER contact sites (MAMs) were assessed by confocal microscopy. NEAT1 knockdown and HK2-VDAC1 interaction studies were performed to explore underlying mechanisms. The N protein induced inflammatory responses, enhanced LPS sensitivity, and triggered mitochondrial dysfunction, ER stress, and MAM formation. It promoted glycolytic reprogramming by upregulating key enzymes (GLUT1, HK2, PKM2). NEAT1 was essential for these effects-N protein increased NEAT1 expression, and NEAT1 knockdown attenuated inflammation, glycolysis, and mitochondrial damage. Mechanistically, NEAT1 silencing restored HK2-VDAC1 association and suppressed VDAC1 oligomerization. The SARS-CoV-2 N protein exacerbates inflammation through a NEAT1-dependent mechanism that drives glycolytic reprogramming and disrupts mitochondrial-ER homeostasis.
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