  The outbreak of the coronavirus disease 2019 (COVID-19) caused by severe
acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has become a worldwide
public health crisis. When the SARS-CoV-2 enters the biological fluids in the
human body, different types of biomolecules (in particular proteins) may adsorb
on its surface and alter its infection ability. Although great efforts have
recently been devoted to the interaction of the specific antibodies with the
SARS-CoV-2, it still remains largely unknown how the other serum proteins
affect the infection of the SARS-CoV-2. In this work, we systematically
investigate the interaction of serum proteins with the SARS-CoV-2 RBD by the
molecular docking and the all-atom molecular dynamics simulations. It is found
that the non-specific immunoglobulin (Ig) indeed cannot effectively bind to the
SARS-CoV-2 RBD while the human serum albumin (HSA) may have some potential of
blocking its infection (to ACE2). More importantly, we find that the RBD can
cause the significant structural change of the Apolipoprotein E (ApoE), by
which SARS-CoV-2 may hijack the metabolic pathway of the ApoE to facilitate its
cell entry. The present study enhances the understanding of the role of protein
corona in the bio-behaviors of SARS-CoV-2, which may aid the more precise and
personalized treatment for COVID-19 infection in the clinic.
