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Proteotyping of SARS-CoV-2 viral peptides in nasal swab simili

ABSTRACT: Detection by tandem mass spectrometry of a specific subset of SARS-CoV-2 viral peptides to illustrate the potential of shotgun proteomics for clinical diagnostic.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Betacoronavirus Sp. (ncbitaxon:1928434)

SUBMITTER: Jean Armengaud

PROVIDER: MSV000086229 | MassIVE | Fri Oct 02 09:17:00 BST 2020

SECONDARY ACCESSION(S): PXD019686

REPOSITORIES: MassIVE

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Publications

Proteotyping SARS-CoV-2 Virus from Nasopharyngeal Swabs: A Proof-of-Concept Focused on a 3 Min Mass Spectrometry Window.

Gouveia Duarte D Miotello Guylaine G Gallais Fabrice F Gaillard Jean-Charles JC Debroas Stéphanie S Bellanger Laurent L Lavigne Jean-Philippe JP Sotto Albert A Grenga Lucia L Pible Olivier O Armengaud Jean J

Journal of proteome research 20200805 11

Rapid but yet sensitive, specific, and high-throughput detection of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in clinical samples is key to diagnose infected people and to better control the spread of the virus. Alternative methodologies to PCR and immunodiagnostics that would not require specific reagents are worthy to investigate not only for fighting the COVID-19 pandemic but also to detect other emergent pathogenic threats. Here, we propose the use of tandem mass spect ...[more]

PMID: 32697082

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Proteotyping of SARS-CoV-2 viral peptides in nasal swab simili

Project description:Detection by tandem mass spectrometry of a specific subset of SARS-CoV-2 viral peptides to illustrate the potential of shotgun proteomics for clinical diagnostic.

2020-07-23 | PXD019686 | Pride

The PDZ-binding motif of SARS-CoV envelope protein is a determinant of viral pathogenesis

Project description:A recombinant SARS-CoV lacking the envelope (E) protein is attenuated in vivo. Here we report that E protein PDZ-binding motif (PBM), a domain involved in protein-protein interactions, is a major virulence determinant in vivo. Elimination of SARS-CoV E protein PBM by using reverse genetics led to attenuated viruses (SARS-CoV-mutPBM) and to a reduction in the deleterious exacerbate immune response triggered during infection with the parental virus (SARS-CoV-wt). Cellular protein syntenin bound E protein PBM during SARS-CoV infection. Syntenin activates p38 MAPK leading to overexpression of inflammatory cytokines, and we have shown that active p38 MAPK was reduced in lungs of mice infected with SARS-CoVs lacking E protein PBM (SARS-CoV-mutPBM) as compared with the parental virus (SARS-CoV-wt), leading to a decreased expression of inflammatory cytokines and to viral attenuation. Therefore, E protein PBM is a virulence factor that activates pathogenic immune response most likely by using syntenin as a mediator of p38 MAPK induced inflammation. Three biological replicates were independently hybridized (one channel per slide) for each sample type (SARS-CoV-wt, SARS-CoV-mutPBM, Mock). Slides were Sure Print G3 Agilent 8x60K Mouse (G4852A-028005)

2014-10-31 | E-GEOD-52920 | biostudies-arrayexpress

Blood RNA-seq data from individuals during the UK Covid-19 lockdown, spanning sequential weeks from first PCR-confirmed SARS-CoV-2 infection, used to evaluate blood transcriptomic signatures of viral infection and identify host-response biomarkers of early SARS-CoV-2 infection

Project description:Healthcare workers were recruited at St Bartholomew’s Hospital, London, UK in the week of lockdown in the United Kingdom (between 23rd and 31st March 2020). Participants underwent weekly evaluation using a questionnaire and biological sample collection (including serological assays) for up to 16 weeks when attending for work and self-declared as fit to attend work at each visit, with further follow up samples collected at 24 weeks. Blood RNA sequencing data was to be used to identify host-response biomarkers of early SARS-CoV-2 infection, to evaluate existing blood transcriptomic signatures of viral infection, and to describe the underlying biology during SARS-CoV-2 infection. This submission includes a total of 172 blood RNA samples from 99 participants. Of these, 114 samples (including 16 convalescent samples collected 6 months after infection) were obtained from 41 SARS-CoV-2 cases, with the remaining 58 from uninfected controls. Participants with available blood RNA samples who had PCR-confirmed SARS-CoV-2 infection during follow-up were included as ‘cases’. Those without evidence of SARS-CoV-2 infection on nasopharyngeal swabs and who remained seronegative by both Euroimmun anti S1 spike protein and Roche anti nucleocapsid protein throughout follow-up were included as uninfected controls. ‘Cases’ include all available RNA samples, including convalescent samples at week 24 of follow-up for a subset of participants. For uninfected controls, we included baseline samples only. Sample class denotes weekly interval to positive SARS-CoV-2 PCR; non-infected controls (NIC); convalescent samples (Conv)_.

2021-07-07 | E-MTAB-10022 | biostudies-arrayexpress

Capturing SARS-cov in low abundant patient samples: a comparative analysis (metagenomics NS).

Project description:In this study, we tested the efficacy of five commercial probes panels at detecting SARS-CoV-2 genome including panels from Illumina, Twist Bioscience and Arbor Bioscience. To do so, we used 19 patient nasal swab samples broken down into 5 series of 4 samples of equivalent SARS-CoV-2 viral load (cycle threshold (CT): low CT means a high viral load – CT26, CT29, CT32, CT35 and CT36+).

2022-06-01 | E-MTAB-11236 | biostudies-arrayexpress

Capturing SARS-cov in low abundant patient samples: a comparative analysis (twist panviral NS).

2022-06-01 | E-MTAB-11237 | biostudies-arrayexpress

Capturing SARS-cov in low abundant patient samples: a comparative analysis (arbo double ms) .

2022-06-01 | E-MTAB-11232 | biostudies-arrayexpress

Capturing SARS-cov in low abundant patient samples: a comparative analysis (Illumina respv NS).

2022-02-08 | E-MTAB-11233 | biostudies-arrayexpress

Capturing SARS-cov in low abundant patient samples: a comparative analysis (Twist sarscov MS).

2022-06-01 | E-MTAB-11234 | biostudies-arrayexpress

Capturing SARS-cov in low abundant patient samples: a comparative analysis (arbo single MS).

2022-06-01 | E-MTAB-11235 | biostudies-arrayexpress

Nanomolar inhibition of SARS-CoV-2 infection by N-terminally extended HR2 peptides

Project description:Variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) challenge currently available COVID-19 vaccines and monoclonal antibody therapies through changes of epitopes on the receptor binding domain of the viral spike glycoprotein (S). Hence, there is a specific urgent need for alternative antivirals that target processes less likely to be affected by mutation, such as the membrane fusion step of viral entry into the host cell. One such antiviral class includes peptide inhibitors which block formation of the HR1HR2 six-helix bundle of the SARS-CoV-2 spike protein and thus interfere with viral membrane fusion; HR2 derived peptides are validated inhibitors of this process. Here, we identify a short N-terminal region that, when appended to the helical region of an HR2 peptide from previous studies, leads to potent inhibition of fusion. The extended peptide shows an ~100-fold increase in efficacy compared with the previously used 36-amino-acid version of HR2, effectively achieving single-digit nanomolar inhibition of SARS-CoV-2 in cell-based fusion, VSV-SARS-CoV-2 chimera, and authentic SARS-CoV-2 infection assays. The peptide also strongly inhibits all major SARS-CoV-2 variants to date. Structural studies of the HR1HR2 bundle reveal the formation of an extended, stabilized N-terminus that interacts with the HR2 triple helix, further stabilizing the HR1HR2 bundle. Together, these results suggest that regions outside the previously studied HR2 helical region may offer new opportunities for potent peptide-derived therapeutics for SARS-CoV-2 and its variants.

2022-09-21 | GSE203229 | GEO

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