Anti-SARS CoV2 Spike S1 Antibody (Clone: ABM1G2.1F7)

The spike (S) protein of nCoV/SARS-CoV-2/COVID-19 is one of the structural glycoproteins that remains embedded in viral envelope and acts as the fundamental component of early viral infection of nCoV/SARS-CoV-2/COVID-19 upon binding the host receptor. The nCoV/SARS-CoV-2/COVID-19 has a trimeric spike protein which has two main domains such as S1 domain for receptor binding and S2 domain for membrane fusion and several specific cleavage sites in S1- S2 boundary junction that needs a novel, endocytic protease- primed cleavage to get activated during infection. It mainly binds to the furin protein on the cell membrane which performs trypsin like proteolytic cleavage and then the protein gets activated facilitating its entry into the host. This transmembrane spike protein of nCoV/SARS-CoV-2/COVID-19 shares binding property to the Angiotensin Converting Enzyme 2 (ACE2) likely to that of SARS- CoV. The high affinity of nCoV/SARS-CoV-2/COVID-19 Spike protein for human ACE2 may contribute to the apparent ease with which nCoV/SARS-CoV-2/COVID-19 can spread from human-to-human and make nCoV/SARS-CoV-2/COVID-19 pandemic. Protein function: [Spike protein S1]: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32221306, PubMed:32075877, PubMed:32155444). Binding to host NRP1 and NRP2 via C-terminal polybasic sequence enhances virion entry into host cell (PubMed:33082294, PubMed:33082293). This interaction may explain virus tropism of human olfactory epithelium cells, which express high level of NRP1 and NRP2 but low level of ACE2 (PubMed:33082293). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270). Uses human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Can be alternatively processed by host furin (PubMed:32362314). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. [The UniProt Consortium]