Analysis Biomolecular Interactions of mAb Pairs with SARS-CoV SB Domain by BLI (CAT#: STEM-MB-0143-CJ)

Introduction

The entry of coronaviruses into host cells is mediated by the transmembrane S glycoprotein, which forms homotrimers that protrude from the viral surface. The S glycoprotein comprises two functional subunits: S1 (divided into A, B, C and D domains), which is responsible for binding to host-cell receptors; and S2, which promotes fusion of the viral and cellular membranes. SARS-CoV-2 S glycoprotein is closely related to the bat SARS-related coronavirus RaTG13 S, with which it shares 97.2% amino acid sequence identity. In humans, angiotensin converting enzyme 2 (ACE2) is a functional receptor for SARS-CoV-2, as also is the case for SARS-CoV-2. Domain B of subunit S1 (SB) is the receptor-binding domain (RBD) of the S glycoprotein, and binds to ACE2 with high affinity, which possibly contributed to the current rapid transmission of SARS-CoV-2 in humans as was previously proposed for SARS-CoV. As the S glycoprotein of coronaviruses mediates entry into host cells, it is the main target of neutralizing antibodies and the focus of efforts to design therapeutic agents and vaccines. The S-glycoprotein trimers are extensively decorated with N-linked glycans that are important for protein folding and modulate accessibility to host proteases and neutralizing antibodies.