COVID – structural research of SARS-CoV-2

Abstract

The appearance and spread of the virus called Severe Acute Respiratory Syndrome Corona Virus 2 (SARS-CoV-2) has changed our life all around the world. It at least upends people’s lives, but it brings human suffering, what is more it kills people. The COVID-19 pandemic is attacking societies at their core. It has quickly developed into a global health crisis resulted in human, economic and social crises. As a response, the COVID-19 pandemic has increased human solidarity. It includes practical help especially for elderly people and other vulnerable groups but it brought even more in science. The rapid spread of the virus urged quick actions towards new therapeutics, vaccines and medicines. Experiencing the enormous impact of this disease, the researchers have adopted open science methods to fight via global collaborative efforts. The openness leads to research acceleration. Open science consists of open access, open data and open source (availability of research publication, research data and liberal licence terms). SARS-CoV-2 related data are being generated and shared, like virus protein structural results and fragment hits. It took 5 years to develop vaccine after the 2014–2016 Ebola virus epidemic. Vaccine development against SARS-CoV-2 took considerably shorter time, 1.5 years. The COVID related research is an example of global cooperation. Unfortunately, SARS-CoV-2 will likely stay with us as a common pathogen. There is a race against viruses, also newmutations remain a constant thread. It substantiates the necessity of the openness, which hopefully will persist in the future in the discovery of newmedicines and chemicals. The RNA genome of SARS-CoV-2 is one of the largest RNA genomes among RNA viruses. The viral RNA of SARS-CoV-2 encodes many proteins. Accessory and nonstructural proteins facilitate the viral infection cycle after infection. Four types of structural proteins are present in the virion to initiate infection and protect the viral RNA: spike-proteins, envelope-protein, membrane-protein and nucleocapsid. DrAndreaThorn, the head of a research teamat the Institute ofNanostructure and Solid State Physics, University of Hamburg, Germany, has contacted Crystallography Reviews at the end of October 2020 with the idea to publish review articles in a thematic issue on structural biology of the structurally known proteins from SARS-CoV and SARS-CoV-2. Now, there are reviews to fill two special issues with the SARS-CoV related structural biology to improve function–structure relations. She and her collaborators are also publishing a series of blog posts with impressive figures and especially animations. SamHorrell from the Diamond Light Source, Didcot, UK; Gianluca Santoni from European Synchrotron Radiation Facility, Grenoble, France and Andrea Thorn report about the ‘Structural biology of SARS-CoV-2 endoribonuclease NendoU (nsp15)’ in Issue 1 of Volume 28 of Crystallography Reviews. Nsp15 has been one of the lesser explored proteins compared to other SARS-CoV-2 proteins. SARS-CoV-2 nsp15 is an RNAuridylate-specific Mn2+-dependent endoribonuclease from the nidoviral endoU (NendoU) family, which acts on single-stranded and double-stranded RNA to help SARS-CoV-2 evade detection