About: Processing of the SARS-CoV pp1a/ab nsp7-10 region

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Processing of the SARS-CoV pp1a/ab nsp7-10 region
Creator	Hilgenfeld, Rolf Falke, Sven Krichel, Boris Redecke, Lars Uetrecht, Charlotte
source	BioRxiv; MedRxiv
abstract	Severe acute respiratory syndrome coronavirus (SARS-CoV) is the causative agent of a respiratory disease with a high case fatality rate. During the formation of the coronaviral replication/transcription complex (RTC), essential steps include processing of the conserved polyprotein nsp7-10 region by the main protease Mpro and subsequent complex formation of the released nsp’s. Here, we analyzed processing of the coronavirus nsp7-10 region using native mass spectrometry showing consumption of substrate, rise and fall of intermediate products and complexation. Importantly, there is a clear order of cleavage efficiencies, which is influenced by the polyprotein tertiary structure. Furthermore, the predominant product is an nsp7+8(2:2) hetero-tetramer with nsp8 scaffold. In conclusion, native MS, opposed to other methods, can expose the processing dynamics of viral polyproteins and the landscape of protein interactions in one set of experiments. Thereby, new insights into protein interactions, essential for generation of viral progeny, were provided, with relevance for development of antivirals.
has issue date	2019-12-03(xsd:dateTime)
bibo:doi	10.1101/860049
has license	medrxiv
sha1sum (hex)	63e827c45330a59cb00188c51e81210d7a611b78
schema:url	https://doi.org/10.1101/860049
resource representing a document's title	Processing of the SARS-CoV pp1a/ab nsp7-10 region
schema:publication	bioRxiv
resource representing a document's body	covid:63e827c45330a59cb00188c51e81210d7a611b78#body_text
is schema:about of	named entity 'SARS-CoV' named entity '1:2' named entity 'nano-electrospray' named entity 'pH 8' named entity 'phosphate' named entity 'SARS-CoV' named entity 'dimer' named entity 'proteolytic processing' named entity 'lysed' named entity 'data analysis' named entity 'nsp5' named entity 'peptides' named entity 'nsp5' named entity 'Thermo Fisher Scientific' named entity 'GE Healthcare' named entity 'substrates' named entity 'cleavage site' named entity 'CID' named entity 'NNE' named entity 'DTT' named entity 'nsp' named entity 'ribosomal' named entity 'intermediate product' named entity 'cleavage site' named entity 'non-covalent interactions' named entity 'stoichiometry' named entity 'mass spectra' named entity 'imidazole' named entity 'Merck Millipore' named entity 'SARS-CoV' named entity 'fluorophore' named entity 'MS/MS' named entity 'stoichiometry' named entity 'DTT' named entity 'protein' named entity 'cleavage site' named entity 'capillaries' named entity 'glycerol' named entity 'nsp' named entity 'mass spectra' named entity 'DTT' named entity 'excitation wavelength' named entity 'Tecan' named entity 'FRET' named entity 'non-covalent interactions' named entity 'covalent' named entity 'chymotrypsin' named entity 'non-covalent interactions' named entity 'Thermo Fisher Scientific' named entity 'FRET' named entity 'micropipette' named entity 'zoonotic infections' named entity 'in-vitro' named entity 'substrates' named entity 'plasmid' named entity 'polar bonds' named entity 'cDNA' named entity 'protease' named entity 'protomers' named entity 'inter-domain' named entity 'FRET' named entity 'NaCl' named entity 'amino-acid residues' named entity 'tetramer' named entity 'DMSO' named entity 'peptide' named entity 'SARS-CoV' named entity 'nsp' named entity 'polyprotein' named entity 'dimerization' named entity 'FRET' named entity 'MS/MS' named entity 'protease' named entity 'polyprotein' named entity 'protein complexes' named entity 'nsp' named entity 'cleavage site' named entity 'fused silica' named entity 'processivity' named entity 'N-terminally'

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