> In this study, conserved domain analysis, homology modeling, and molecular docking were used In other words, they haven't actually done any experiments. > T

> In this study, conserved domain analysis, homology modeling, and molecular docking were used In other words, they haven't actually done any experiments. > The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively. At the same time, orf1ab, ORF10, and ORF3a proteins could coordinate attack the heme on the 1-beta chain of hemoglobin to dissociate the iron to form the porphyrin. Haemoglobin is inside red blood cells. If you think these interactions are happening, you need to explain how you think the viral proteins are getting inside red blood cells in sufficient quantity to significantly screw up the haemoglobin. I don't think red blood cells even express ACE2, the receptor the virus uses to enter cells. If viruses did somehow manage to enter red blood cells, they would find that there is no transcription and translation machinery (red blood cells aren't really cells, psych!), and so they won't be able to make more of their proteins - the only things doing any interacting will be the scant handful of proteins that the virus particles brought with them. Even then, the paper is really unclear on the details, but i get the impression that it is the extracellular domains of the envelope protein and surface glycoprotein that are being modelled. When a virus enters a cell, it does it by fusing its envelope with the membrane of the host cell, which leaves the extracellular domains of the viral membrane proteins on the outside of the host cell. Which is not where the haemoglobin is. I think this paper is absolute nonsense from top to bottom. What am i missing?