The specific structure of this protein was solved and can now be used to rationally design effective anti-2019-nCoV therapies, vaccines, and diagnostic tests; however three potential antibodies that were tested by the authors were not effective.
Wrapp, D. et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science (2020). DOI: 10.1126/science.abb2507
13 March 2020
When viruses enter their target cell in the human body, they identify it by using a unique binding protein on their surface that has a high affinity for a receptor on the cell. For 2019-nCoV, this binding protein is a trimeric spike glycoprotein, or a three-part molecule containing both carbohydrate- and protein-based components. It binds to its target receptor on a human cell, angiotensin-converting enzyme 2 (ACE2), with 10 times greater affinity than does the equivalent spike protein of SARS-CoV. Then, it undergoes a change in shape allowing the virus to fuse with the cell and for viral machinery to enter inside. The authors elicited a 3.5-angstrom resolution structure of the spike protein using cryo-electron microscopy. They tested three known monoclonal antibodies to SARS-CoV for cross-reactivity with 2019-nCoV, however the results were unsuccessful with no binding detected. Having a clear understanding of this structure enables researchers to develop therapies, vaccines, and diagnostic tests that can more specifically target this key element of the virus.
Summary by: Tatiana Yeuchyk