Abstract
A novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified as the cause of the COVID-19 pandemic that originated in China in December 2019. Although extensive research has been performed on SARS-CoV-2, the binding behavior of spike (S) protein and receptor binding domain (RBD) of SARS-CoV-2 at different environmental conditions have yet to be studied. The objective of this study is to investigate the effect of temperature, fatty acids, ions, and protein concentration on the binding behavior and rates of association and dissociation between the S protein and RBD of SARS-CoV-2 and the hydrophobic aminopropylsilane (APS) biosensors using biolayer interferometry (BLI) validated with molecular dynamics simulation. Our results suggest three conditions—high ionic concentration, presence of hydrophobic fatty acids, and low temperature—favor the attachment of S protein and RBD to hydrophobic surfaces. Increasing the temperature within an hour from 0 to 25 °C results in S protein detachment, suggesting that freezing can cause structural changes in the S protein, affecting its binding kinetics at higher temperature. At all the conditions, RBD exhibits lower dissociation capabilities than the full-length S trimer protein, indicating that the separated RBD formed stronger attachment to hydrophobic surfaces compared to when it was included in the S protein.
Highlights
A novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified as the cause of the COVID-19 pandemic that originated in China in December 2019
Little is known about the binding behavior and macromolecular interactions of S protein and receptor binding domain (RBD) of SARS-CoV-2 at different conditions—low temperatures, high humidity, and presence of fatty acids—that are typical in critical infrastructures such as meat processing facilities
All the other three S protein concentrations had minimal to no detachment, meaning that the S protein was not able to resuspend into the ionic environment once it bound to the hydrophobic surface
Summary
A novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified as the cause of the COVID-19 pandemic that originated in China in December 2019. The objective of this study is to investigate the effect of temperature, fatty acids, ions, and protein concentration on the binding behavior and rates of association and dissociation between the S protein and RBD of SARS-CoV-2 and the hydrophobic aminopropylsilane (APS) biosensors using biolayer interferometry (BLI) validated with molecular dynamics simulation. Shang et al provided the crystal structure of the RBD of the S protein in complex with ACE2 and discovered that the binding affinity of RBD to ACE2 was higher in SARS-CoV-2 than that in SARS-CoV due to the unique structural features of SARS-CoV-217 Their team further identified the key mechanism of SARS-CoV-2 cell entry by investigating its receptor binding and protease activation of the s pike[18]. As an attempt to develop vaccines during the early stage of COVID-19, a study used BLI to discover a cross-reactive human IgA monoclonal antibody MAb362 which binds to S proteins of SARS-CoV and SARS-CoV-2 and blocks ACE2 receptor binding by overlapping the binding e pitope[32]
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