Structural on-site analysis of SARS-CoV-2 protein S reveals the existence of "hinges" that allow flexibility

Structural on-site analysis of SARS-CoV-2 protein S reveals the existence of "hinges" that allow flexibility

ProteinSpikeSARS-CoV-2 (S) allows the virus to enter the host cell by binding to the angiotencin II (ACE2) converting enzyme receptor and is a major target for neutralizing antibodies. About 20 to 40 spines decorate the surface of the virus. Turo-ováet al.it now shows that this protein is flexibly linked to the surface of the virus, using 3 "hinges" that are well protected by glycosylation sites. The flexibility conferred by these 3 hinges could explain how multiple S proteins can act in concert to bind to the flat surface of the host cell.

In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein enables viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor and is a major target for neutralizing antibodies. About 20 to 40 spikes decorate the surface of virions. Turoňováet al.now show that the spike is flexibly connected to the viral surface by three hinges that are well protected by glycosylation sites. The flexibility imparted by these hinges may explain how multiple spikes act in concert to engage onto the flat surface of a host cell.

Source: science.sciencemag.org