Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

NSP3 (1)


SARS-CoV-2 Proteins
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    Comparative host interactomes of the SARS-CoV-2 nonstructural protein 3 and human coronavirus homologs

    Authors: Katherine M Almasy; Jonathan P Davies; Lars Plate

    doi:10.1101/2021.03.08.434440 Date: 2021-03-08 Source: bioRxiv

    Human coronaviruses have become an increasing threat to global health; three highly pathogenic strains have emerged since the early 2000s, including most recently SARS-CoV-2, the cause of COVID-19 MESHD. A better understanding of the molecular mechanisms of coronavirus pathogenesis is needed, including how these highly virulent strains differ from those that cause milder, common-cold like disease. While significant progress has been made in understanding how SARS-CoV-2 proteins interact with the host cell, non-structural protein 3 PROTEIN ( nsp3 HGNC) has largely been omitted from the analyses. Nsp3 HGNC is a viral protease with important roles in viral protein biogenesis, replication complex formation, and modulation of host ubiquitinylation and ISGylation. Herein, we use affinity purification-mass spectrometry to study the host-viral protein-protein interactome of nsp3 HGNC from five coronavirus strains: pathogenic strains SARS-CoV-2, SARS-CoV MESHD, and MERS-CoV; and endemic common-cold strains hCoV-229E and hCoV-OC43. We divide each nsp3 HGNC into three fragments and use tandem mass tag technology to directly compare the interactors across the five strains for each fragment. We find that few interactors are common across all variants for a particular fragment, but we identify shared patterns between select variants, such as ribosomal proteins enriched in the N-terminal fragment ( nsp3 HGNC.1) dataset for SARS-CoV-2 and SARS-CoV MESHD. We also identify unique biological processes enriched for individual homologs, for instance nuclear protein important for the middle fragment of hCoV-229E, as well as ribosome biogenesis of the MERS nsp3 HGNC.2 homolog. Lastly, we further investigate the interaction of the SARS-CoV-2 nsp3 HGNC N-terminal fragment with ATF6 HGNC, a regulator of the unfolded protein response. We show that SARS-CoV-2 nsp3 HGNC.1 directly binds to ATF6 HGNC and can suppress the ATF6 HGNC stress response. Characterizing the host interactions of nsp3 HGNC widens our understanding of how coronaviruses co-opt cellular pathways and presents new avenues for host-targeted antiviral therapeutics.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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