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{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7205724","sourcedb":"PMC","sourceid":"7205724","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7205724","text":"2 SARS-CoV2 cell entry is not complex\nFig. 1 is a schematic illustration of the minimum proteins required to mediate the SARS-CoV2 cell entry. The trimeric, transmembrane spike (S) glycoprotein of the virus, SARS-2-S, includes two main functional subunits: S1 and S2. The former, in turn, consists of the four core domains, S1A, S1B, S1C, and S1D, that contribute to the attachment to the surface receptor of target cells. Then, the latter coordinates the fusion of viral and cellular membranes. Receptor binding activates proteases that can carry out proteolytic cleavage of the S protein. In coronaviruses, cleavage occurs at two sites: the S1/S2 junction and at the S2′, a region close to the viral fusion peptide [2]. Proteolytic cleavage of the S protein causes conformational changes so that they cannot revert to the original structure and profound enough to prime the S2 subunit for the fusion of viral and cellular membranes.\nFig. 1 Proteins required for the SARS-CoV2-cell 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