Good news! Human ingenuity beats pathogens any time!
"... Genetic instructions in our cells are transcribed from DNA to messenger RNA (mRNA), then translated into proteins that enable functions such as cell-to-cell communication. After translation, these proteins often need additional modifications, called post-translational modifications, to ensure they perform effectively. SUMOylation is one such post-translational modification that directly regulates viral replication and the body’s innate immune response. ...
A core component of the SARS-CoV-2 virus is the nucleocapsid (N) protein, mainly responsible for packaging RNA in a protective covering. SUMOylation directs the virus’ N protein to the right location for packaging after it infects human cells. Once it’s in the right place, the protein begins inserting copies of its genes into new infectious virus particles, virions, which spread and make us sicker. ..."
"... Using similar methods, the bioengineering team previously discovered that the two most common types of flu virus, Influenza A and Influenza B, require the same post-translational SUMOylation modification in order to replicate. ..."
From the abstract:
"Viruses, such as Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), infect hosts and take advantage of host cellular machinery for genome replication and new virion production. Identifying and elucidating host pathways for viral infection is critical for understanding the development of the viral life cycle and novel therapeutics. The SARS-CoV-2 N protein is critical for viral RNA (vRNA) genome packaging in new virion formation. Using our quantitative Förster energy transfer/Mass spectrometry (qFRET/MS) coupled method and immunofluorescence imaging, we identified three SUMOylation sites of the SARS-CoV-2 N protein. We found that (1) Small Ubiquitin-like modifier (SUMO) modification in Nucleocapsid (N) protein interaction affinity increased, leading to enhanced oligomerization of the N protein; (2) one of the identified SUMOylation sites, K65, is critical for its nuclear translocation. These results suggest that the host human SUMOylation pathway may be critical for N protein functions in viral replication and pathology in vivo. Thus, blocking essential host pathways could provide a novel strategy for future anti-viral therapeutics development, such as for SARS-CoV-2 and other viruses."
Scientists uncover COVID’s weakness (main news source) Without key proteins, virus cannot infect people
Graphical abstract
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