Infectious Diseases

SARS-CoV-2 Entry Point Structure Identified by Electron Microscopy

Posted on 17 March 2020

Researchers at Westlake University, Zhejiang Province, have used cryogenic electron microscopy to identify the full structure of ACE2 – the protein that SARS-CoV-2 uses to enter human cells.

Representation of the ACE2 complex, showing the interaction with the coronavirus S protein (pictured right)
Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q. (2020). Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2. Science, eabb2762. doi: 10.1126/science.abb2762

Unlike bacteria, viruses cannot replicate by themselves, and must instead enter a host cell to hijack its replication machinery. In order to gain access to human cells, SARS-CoV-2 binds to angiotensin converting enzyme 2 (ACE2) – an enzyme which is highly expressed in the lungs. Once bound, the virus then fuses with the cell membrane and enters the cytoplasm.

The study, published in Science, also compared how SARS-CoV and SARS-CoV-2 interface with the enzyme. Deepening our understanding of how the virus interacts with its entry point may aid the development of treatments, according to the authors:

Our findings not only shed light on the mechanistic understanding of viral infection, but will also facilitate development of viral detection techniques and potential antiviral therapeutics.

SARS-CoV-2 Point of Entry Into Cells Captured by Cryo-EM. (2020). Retrieved 17 March 2020, from


Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2: DOI: 10.1126/science.abb2762

SARS-CoV-2 Point of Entry Into Cells Captured by Cryo-EM:

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