SPR analysis on the interactions between heparin and SARS-CoV-2 spike protein RBDs from different variants

ABSTRACT

The COVID-19 pandemic has become a major human health concern. The pathogen responsible for COVID-19, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), invades its host through the interaction of its spike (S) protein with a host cell receptor, angiotensin-converting enzyme 2 (ACE2). In addition to ACE2, heparan sulfate (HS) on the surface of host cells also plays a significant role as a co-receptor. In this study, SARS-CoV-2 SP receptor binding domain (RBD) wild type (WT), Delta and Omicron variants were expressed in Expi293F cells and used in the kinetic and structural analysis on their interactions with heparin by Surface plasminogen resonance (SPR). Detailed kinetic and structural analysis of the interactions of SARS-CoV-2 SP RBDs with heparin provides important information for designing anti-SARS-CoV-2 molecules.