Israeli scientists at Hebrew University of Jerusalem report in Cell Reports that the SARS‑CoV‑2 nucleocapsid protein (NP)—key to viral assembly—can detach from infected cells and bind to surface glycosaminoglycans (heparan sulfate proteoglycans) on adjacent healthy epithelial cells . This misplacement causes anti‑NP antibodies to misidentify these uninfected cells as threats, activating the classical complement pathway and provoking inflammation and tissue injury—a mechanism potentially linked to aggravated Covid‑19 and long Covid drivers .
Crucially, the anticoagulant enoxaparin, a heparin analog, outcompetes NP for these binding sites, effectively blocking its attachment in vitro and in patient samples. Lab tests confirmed that enoxaparin prevented antibody‑mediated complement attacks, suggesting a promising new therapeutic route to reduce immune‑driven damage in Covid‑19.
Meanwhile, Omicron’s NB.1.8.1 variant—first identified in January 2025—is being monitored by the World Health Organization. Detected in over 22 countries, it now constitutes 10.7 % of recent global sequences, up from 2.5 % in late April.
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NB.1.8.1 carries spike‑protein mutations potentially enhancing transmission and antibody evasion, but current evidence indicates it doesn’t cause more severe disease. Vaccines remain effective at preventing serious illness.
This study advances understanding of NP‑induced complement activation and highlights enoxaparin as a potential mechanism for preventing immune‑mediated tissue damage—offering fresh hope amid the rise of variants like NB.1.8.1.
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