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Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2.

Qihui Wang1, Yanfang Zhang2, Lili Wu3

  • 1CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen 518112, China; CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.

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The SARS-CoV-2 spike protein binds human ACE2 with higher affinity due to key residue changes. Antibodies effective against SARS-CoV do not bind SARS-CoV-2, highlighting viral differences.

Keywords:
ACE2CTDSARS-CoV-2crystal structureimmunogenicityreceptorreceptor binding domain

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The novel coronavirus (SARS-CoV-2) emerged, causing global health concerns.
  • Angiotensin-converting enzyme 2 (ACE2) is identified as the entry receptor for SARS-CoV-2.
  • Understanding the interaction between SARS-CoV-2 and ACE2 is crucial for therapeutic development.

Purpose of the Study:

  • To determine the crystal structure of the SARS-CoV-2 C-terminal domain (CTD) spike protein bound to human ACE2 (hACE2).
  • To elucidate the molecular basis of SARS-CoV-2 binding to hACE2 and compare it with SARS-CoV.
  • To investigate the antigenic differences between SARS-CoV and SARS-CoV-2 spike proteins.

Main Methods:

  • X-ray crystallography was used to obtain the structure of the SARS-CoV-2 CTD-hACE2 complex.
  • Structural analysis focused on the binding interface to identify key interactions and residue differences.
  • Antibody binding assays were performed using monoclonal and polyclonal antibodies against SARS-CoV spike protein.

Main Results:

  • The crystal structure revealed a hACE2-binding mode similar to SARS-CoV but with key residue substitutions in SARS-CoV-2-CTD.
  • These substitutions result in a slightly stronger interaction and higher binding affinity of SARS-CoV-2 to hACE2 compared to SARS-CoV.
  • Murine antibodies against SARS-CoV spike protein/receptor-binding domain (RBD) did not interact with SARS-CoV-2 spike protein, indicating distinct antigenicity.

Conclusions:

  • The structural and binding data provide insights into the enhanced receptor binding of SARS-CoV-2.
  • Differences in antigenicity suggest that existing antibodies against SARS-CoV may not be effective against SARS-CoV-2.
  • These findings are vital for understanding viral pathogenesis and developing targeted therapeutic strategies against SARS-CoV-2.