Abstract

A team of researchers in China have reported the crystal structure of the novel coronavirus, SARS-CoV-2, bound to its target on human cells (Science 2020, DOI: 10.1126/science.abb2762). The interaction (shown), captured through cryogenic electron microscopy by Qiang Zhou of the Westlake Institute for Advanced Study and colleagues, reveals some of the chemistry behind how the coronavirus hijacks angiotensin-converting enzyme 2 (ACE2). The researchers think the structure could lead to the development of antibodies that block this interaction. Jason McLellan, the University of Texas at Austin researcher who led the team that recently revealed the structure of the coronavirus’s spike protein, says the work of Zhou’s team will help scientists better understand how coronaviruses use this blood pressure–regulating enzyme to get into human cells. ACE2 helps convert the hormone angiotensin into its active form, which makes blood vessels contract. The SARS-CoV-2 spike protein has two elements involved in infecting human cells.

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