Immediately after the infection of a cell in the throat or lungs, the SARS-CoV-2 virus works very hard to replicate, using the human cell's metabolic pathways to produce its proteins and make sure that its genetic material (the RNA genome) is copied. The RNA genome is then packaged very compactly into new virus particles that are released from the cell to infect more cells.
, called the nucleocapsid protein , is particularly important for rapid and efficient replication. It wraps around the RNA genome in the virus and ensures that the very long RNA is tightly coiled up. When it penetrates the cell, N detaches itself from the RNA genome and assumes a whole range of functions duringWhen the RNA is translated into viral proteins, N protects the RNA from being destroyed by the cell's antiviral defense mechanism .
Like a Swiss army knife, N has several tools at its disposal for all these functions: Firstly, N must be able to distinguish between cellular and viral RNA and to coil up the latter in a spiral shape. That is why N can bind viral RNA in a relatively non-specific manner. To steer the transcription of viral RNA into viral proteins , for example, N must, however, equally be able to recognize specific positions on the viral RNA, called RNA motifs.
Researchers led by Dr. Sophie Korn and Dr. Andreas Schlundt from the Institute for Molecular Biosciences and the Center for Biomolecular Magnetic Resonance at Goethe University Frankfurt have now shed light on exactly how this specific binding through one of N's tools, known as the N-terminal domain , works. Their results build on preliminary studies by the COVID19-NMR consortium established in Frankfurt during the pandemic.
Belgique Dernières Nouvelles, Belgique Actualités
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