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Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2

Pengcheng Han1, Linjie Li2, Sheng Liu3

  • 1CAS Key Laboratory of Pathogen Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China; School of Medicine, Zhongda Hospital, Southeast University, NanJing 210009, China.

Cell
|January 30, 2022
PubMed

Insights

The Omicron variant

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The COVID-19 pandemic persists globally, driven by emerging SARS-CoV-2 variants.
  • Omicron (B.1.1.529) is a significant variant of concern (VOC) due to numerous mutations in its spike protein's receptor-binding domain (RBD).

Purpose of the Study:

  • To investigate the binding characteristics of VOC RBDs with human ACE2 (hACE2).
  • To elucidate the structural mechanisms underlying Omicron and Delta variant RBD interactions with hACE2.

Main Methods:

  • Crystallography and cryo-electron microscopy were employed to resolve the structures of Omicron RBD-hACE2 and Delta RBD-hACE2 complexes.
  • Binding affinities between various VOC RBDs and hACE2 were quantitatively assessed.

Main Results:

  • Omicron RBD exhibits binding affinity to hACE2 comparable to the prototype SARS-CoV-2 RBD, unlike Alpha, Beta, and Gamma variants.
  • Structural analyses reveal how specific mutations in Omicron and Delta RBDs influence hACE2 binding.

Conclusions:

  • The binding profile of Omicron RBD suggests a potential balance between immune evasion and transmissibility.
  • Structural insights into RBD-hACE2 interactions provide a foundation for understanding variant infectivity and developing targeted therapeutics.
Keywords:
RBDVOCsdeltahACE2omicronreceptor-binding domainstructurevariants of concern

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