novel corona virus, 2019-nCoV, SARS-2, with disease, Covid-19

SARS (1) attaches to the cells receptor ACE (1)

SARS-2 attaches to the cells receptor ACE-2

ACE - Angiotensin Converting Enzyme

ACE inhibitors are used to treat high blood pressure (calcium channel blockers).

According to the Mayo Clinic, these medications keep calcium from entering the cell walls of the heart and blood vessels.

SARS attaches to the calcium channel and hyper stimulates the cell into a frenzie of activety. A calcium channel blocker blocks calcium to calm the cell down and lower blood pressure.

SARS-2, novel corona virus, attaches to a different receptor, the ACE-2, which is the oil based vitamin D receptor. This extra oil at the binding site makes the nCoV more strongly attached due to the oil properties.

--------- A medical paper published August 2018 about SARS-CoV, the ACE2 receptor, and trypsin


2018 Aug 13;14(8):e1007236. doi: 10.1371/journal.ppat.1007236. eCollection 2018 Aug.

Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.


The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.
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