User:Andre Wu Le Chun/Sandbox 1: Difference between revisions

<scene name='84/844931/6vsb/2'>6vsb</scene> is a homotrimer transmembrane glycoprotein(S) protruding from the viral surface¹. It is composed by two subunits that are fundamental for the virus entry in the cell: The S1 subunit, a v shaped subunit which contains the receptor binding domain (<scene name='84/844931/S_receptor-binding_domain/1'>RBD</scene>), is responsible for binding to the host cell receptor, and the S2 subunit, responsible for fusion of the viral and cellular membranes. In order to allow the binding of the RBD in S1 with the host cell, the spike protein goes through conformational changes that make the binding domain assume a up conformation, thus, exposing the spike protein to its target receptor.

Due to its role in the infection process, the spike glyprotein may be a potential target of studies that seek methods of preventing COVID-19. These include the development of vaccines based on antibodies that are able to block protein's structure of the protein and on it's recognition/biding mechanisms. For instance, avoiding the cleavage of the furin, located on the B domain of the protein, by the host's proteases could be a way of viral inhibition. Comprehending how the protein can be bound to antibodies could also help the scientific community to prepare for future SARS coronavirus outbreaks that may happen in the future.