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. 2022 May 11;14(5):1029. doi: 10.3390/v14051029

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© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Structures of losartan carboxylic acid (EXP3174), BisA and BisD. The multibasic cleavage site of SARS-CoV-2 (P681R682R683A684R685S686) is a treatment target for negatively charged groups or molecules such as ARBs that possibly target the basic cleavage site, preventing furin cleavage which triggers infection. SARS-CoV-2 Spike (S) Protein consists of two subunits, the surface subunit (S1) and a membrane-anchored subunit (S2). The S1 subunit contains an N-terminal signal peptide (SP), an N-terminal domain (NTD) a receptor-binding domain (RBD) and inside that the receptor-binding motif (RBM). The S2 subunit comprises domains required for membrane fusion, the fusion peptide (FP), two heptad repeats (HR1, HR2), a transmembrane domain (TM) and a cytoplasmic tail (CT). The S1/S2 cleavage site is located at the border between the S1 and S2 subunits (R685-S686).