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Atmospheric Measurement Techniques ; 14(9):6057-6082, 2021.
Article in English | ProQuest Central | ID: covidwho-1413103


The TOPAS (Tikhonov regularised Ozone Profile retrievAl with SCIATRAN) algorithm to retrieve vertical profiles of ozone from space-borne observations in nadir-viewing geometry has been developed at the Institute of Environmental Physics (IUP) of the University of Bremen and applied to the TROPOspheric Monitoring Instrument (TROPOMI) L1B spectral data version 2. Spectral data between 270 and 329 nm are used for the retrieval. A recalibration of the measured radiances is done using ozone profiles from MLS/Aura. Studies with synthetic spectra show that individual profiles in the stratosphere can be retrieved with an uncertainty of about 10 %. In the troposphere, the retrieval errors are larger depending on the a priori profile used. The vertical resolution above 18 km is about 6–10 km, and it degrades to 15–25 km below. The vertical resolution in the troposphere is strongly dependent on the solar zenith angle (SZA). The ozone profiles retrieved from TROPOMI with the TOPAS algorithm were validated using data from ozonesondes and stratospheric ozone lidars. Above 18 km, the comparison with sondes shows excellent agreement within less than ±5 % for all latitudes. The standard deviation of mean differences is about 10 %. Below 18 km, the relative mean deviation in the tropics and northern latitudes is still quite good, remaining within ±20 %. At southern latitudes, larger differences of up to +40 % occur between 10 and 15 km. The standard deviation is about 50 % between 7–18 km and about 25 % below 7 km. The validation of stratospheric ozone profiles with ground-based lidar measurements also shows very good agreement. The relative mean deviation is below ±5 % between 18–45 km, with a standard deviation of 10 %. TOPAS retrieval results for 1 d of TROPOMI observations were compared to ozone profiles from the Microwave Limb Sounder (MLS) on the Aura satellite and the Ozone Mapping and Profiler Suite Limb Profiler (OMPS-LP). The relative mean difference was found to be largely below ±5 % between 20–50 km, except at very high latitudes.

Nat Commun ; 12(1): 542, 2021 01 22.
Article in English | MEDLINE | ID: covidwho-1044339


There is need for effective and affordable vaccines against SARS-CoV-2 to tackle the ongoing pandemic. In this study, we describe a protein nanoparticle vaccine against SARS-CoV-2. The vaccine is based on the display of coronavirus spike glycoprotein receptor-binding domain (RBD) on a synthetic virus-like particle (VLP) platform, SpyCatcher003-mi3, using SpyTag/SpyCatcher technology. Low doses of RBD-SpyVLP in a prime-boost regimen induce a strong neutralising antibody response in mice and pigs that is superior to convalescent human sera. We evaluate antibody quality using ACE2 blocking and neutralisation of cell infection by pseudovirus or wild-type SARS-CoV-2. Using competition assays with a monoclonal antibody panel, we show that RBD-SpyVLP induces a polyclonal antibody response that recognises key epitopes on the RBD, reducing the likelihood of selecting neutralisation-escape mutants. Moreover, RBD-SpyVLP is thermostable and can be lyophilised without losing immunogenicity, to facilitate global distribution and reduce cold-chain dependence. The data suggests that RBD-SpyVLP provides strong potential to address clinical and logistic challenges of the COVID-19 pandemic.

Antibodies, Viral/immunology , COVID-19 Vaccines/immunology , COVID-19/prevention & control , Peptides/immunology , SARS-CoV-2/immunology , Spike Glycoprotein, Coronavirus/immunology , Angiotensin-Converting Enzyme 2/immunology , Animals , Antibodies, Blocking/immunology , Antibodies, Monoclonal/immunology , Antibodies, Neutralizing/immunology , COVID-19/immunology , Cell Line , Mice , Mice, Inbred BALB C , Mice, Inbred C57BL , Protein Interaction Domains and Motifs , Protein Multimerization , Swine
PLoS Biol ; 18(12): e3001016, 2020 12.
Article in English | MEDLINE | ID: covidwho-992640


SARS Coronavirus 2 (SARS-CoV-2) emerged in late 2019, leading to the Coronavirus Disease 2019 (COVID-19) pandemic that continues to cause significant global mortality in human populations. Given its sequence similarity to SARS-CoV, as well as related coronaviruses circulating in bats, SARS-CoV-2 is thought to have originated in Chiroptera species in China. However, whether the virus spread directly to humans or through an intermediate host is currently unclear, as is the potential for this virus to infect companion animals, livestock, and wildlife that could act as viral reservoirs. Using a combination of surrogate entry assays and live virus, we demonstrate that, in addition to human angiotensin-converting enzyme 2 (ACE2), the Spike glycoprotein of SARS-CoV-2 has a broad host tropism for mammalian ACE2 receptors, despite divergence in the amino acids at the Spike receptor binding site on these proteins. Of the 22 different hosts we investigated, ACE2 proteins from dog, cat, and cattle were the most permissive to SARS-CoV-2, while bat and bird ACE2 proteins were the least efficiently used receptors. The absence of a significant tropism for any of the 3 genetically distinct bat ACE2 proteins we examined indicates that SARS-CoV-2 receptor usage likely shifted during zoonotic transmission from bats into people, possibly in an intermediate reservoir. Comparison of SARS-CoV-2 receptor usage to the related coronaviruses SARS-CoV and RaTG13 identified distinct tropisms, with the 2 human viruses being more closely aligned. Finally, using bioinformatics, structural data, and targeted mutagenesis, we identified amino acid residues within the Spike-ACE2 interface, which may have played a pivotal role in the emergence of SARS-CoV-2 in humans. The apparently broad tropism of SARS-CoV-2 at the point of viral entry confirms the potential risk of infection to a wide range of companion animals, livestock, and wildlife.

Angiotensin-Converting Enzyme 2/metabolism , SARS-CoV-2/physiology , Spike Glycoprotein, Coronavirus/metabolism , Viral Tropism , Virus Attachment , Amino Acid Substitution , Animals , Binding Sites , Cats , Cattle , Dogs , Guinea Pigs , HEK293 Cells , Host-Pathogen Interactions , Humans , Rabbits , Rats , Viral Zoonoses/virology