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brow42's picture
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A summary article said that this is a known protein that helps the virus evade the host immune system, and that a similar mutation in SARS-COV-1 resulted in a less virulent infection.

I was wondering if the scientists could comment on this rapid-release paper https://jvi.asm.org/content/jvi/early/2020/04/30/JVI.00711-20.full.pdf

The paper is not easy for me to read. A deletion of 27 amino acids was observed in a patient. Perhaps the scientists could comment on the resulting structural change?

bkoep's picture
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Signal peptide

I don't know the details about this particular protein, but it looks like that deletion mostly includes a "signal peptide," and is more likely to affect the spatial distribution of the protein than the protein's fold.

A signal peptide directs a protein to the cell membrane, and is usually included on membrane-embedded proteins or proteins that need to be secreted from the cell. The signal peptide itself tends to be disordered, and in many cases it is eventually cleaved from the rest of the protein.

So my guess is that removing this peptide probably won't affect how the rest of the protein folds, and more likely affects how the protein is distributed (cytosolic, membrane-embedded, secreted, etc.).


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