The spike (S) glycoprotein of coronaviruses is located on the surface of SARS-CoV-2, commonly known as the Coronavirus. It is known to be essential in the binding of the virus to the host cell at the advent of the infection process. In its native form it is a homo trimer and it is located in the phospholipid membrane of the virus. Hence, to purify S in its native form, the homo trimer needs to be kept intact.
It contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. It’s been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The S protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.
The main functions for the Spike protein are summarized as:
Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component is to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.