Spike-heparan sulfate interactions in SARS-CoV-2 infection

Recent biochemical, biophysical, and genetic studies have shown that heparan sulfate, a major component of the cellular glycocalyx, participates in infection of SARS-CoV-2 by facilitating the so-called open conformation of the spike protein, which is required for binding to ACE2. This review highlights the involvement of heparan sulfate in the SARS-CoV-2 infection cycle and argues that there is a high degree of coordination between host cell heparan sulfate and asparagine-linked glycans on the spike in enabling ACE2 binding and subsequent infection. The discovery that spike protein binding and infection depends on both viral and host glycans provides insights into the evolution, spread and potential therapies for SARS-CoV-2 and its variants.

Automated summary

Heparan sulfate, a major component of the cellular glycocalyx, plays a crucial role in the infection cycle of SARS-CoV-2. It facilitates the open conformation of the spike protein, enabling its binding to ACE2. The coordination between viral and host glycans on the spike protein is essential for the binding and subsequent infection.