https://orcid.org/0000-0002-1918-2970
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Abstract
Following infection, SARS-CoV-2’s leader protein nsp1 is the very first viral protein to be expressed. Its sequence is highly conserved among different SARS-CoV-2 strains, indicating its vital function that makes it a promising target for drugs and vaccination. Nsp1 takes over the host cell protein expression machinery to facilitate the production of SARS-CoV-2 virions by the host cell by binding to the ribosome and obstructing the expression of any but the viral proteins. To date, 28 structures obtained by cryo-electron microscopy and X-ray diffraction have been published, showing the protein’s structural features as well as a number of interactions with host ribosomes. Nsp1 has also been shown to interfere with immune response pathways and is connected to the cytokine storm causing organ damage and failure in COVID-19 patients.
Acknowledgements
The authors would also like to thank Rosemary Wilson for support and discussion and Gianluca Tomasello for his assistance with the reviews’ illustrations. All figures are courtesy of the Coronavirus Structural Task Force (insidecorona.net), which retains copyright for both the text and the figures.
Disclosure statement
No potential conflict of interest was reported by the author(s).
Subject index
Additional information
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Notes on contributors
Johannes Kaub
Johannes Kaub studied chemistry at RWTH Aachen University, with a focus on solid-state physical chemistry. At the Max Planck Institute for the Structure and Dynamics of Matter, he took a dive into cellular biology and laser physics. He supports the Coronavirus Structural Task Force as scientific coordinator with his talent for organization and solving problems. Other than science, his greatest passion is the written word, which is why he is also an editorial board member for the well-known German table top RPG.
Toyin Akinselure
Toyin Akinselure is a microbiologist and presently an MSc student in nanoscience with a focus on nanobiology and nanochemistry at Universität Kassel. She is interested in scientific research, especially in protein chemistry and drug discovery. In autumn and winter 2020, she interned with two research projects, one in drug discovery and the other in protein structure. She found these exciting and hopes to broaden her knowledge in these, perhaps with a master’s thesis. In the Task Force, she put her knowledge in microbiology and nanobiology to some good use especially with outreach and writing blog posts. She is also passionate about communication and engaging in insightful conversations which is why she also hosts her own online video channel.
Lea von Soosten
Lea C. von Soosten is a physics doctoral student at the University Medical Center Hamburg-Eppendorf (UKE) with a focus on biophysics. She is interested in everything related to biology, especially proteins. She joined the Coronavirus Structural Task Force as a student assistant during her Master’s studies to broaden her knowledge in biochemistry and assist the team with literature research. Besides this, she is an up-and-coming artist with a growing enthusiasm for scientific illustrations.
Gianluca Santoni
Gianluca Santoni is a scientist at the European Synchrotron radiation facility. His work is focused on the development of methods for synchrotron serial crystallography, from the comparison of datasets for multi-crystal data collection methods, to the implementation of new measurement techniques at synchrotron beamlines. He got his PhD in structural biology studying the structure of acetylcholinesterase in complex with organophosphate nerve agents, applying a mixture of crystallography and computational methods. More recently he has been involved in the data strategies implementation for open science, participating in activities concerning the storage of experimental metadata, the distribution of raw data along with publication according to FAIR principle, and the definition of the Gold standard format for protein diffraction data. His work with the Coronavirus Structural Task Force has been focused on the implementation of routines to evaluate the quality of both deposited datasets and models.
Andrea Thorn
Dr. Andrea Thorn is a specialist for structure solution by crystallography and Cryo-EM, having contributed to programs such as SHELX, ANODE and PHASER in the past. Her group at the Universität Hamburg develops AI-based methods in crystallography such as the diffraction diagnostics tool AUSPEX and a neural network for secondary structure annotation of Cryo-EM maps (HARUSPEX). Her methods enable other scientists to solve new structures and to answer challenging biological questions. Andrea is very passionate about structural biology and good at bringing people together. She started and leads the Coronavirus Structural Task Force.