Corpus overview


Overview

MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinE (3)


Filter

Genes
Diseases
SARS-CoV-2 Proteins
    displaying 1 - 3 records in total 3
    records per page




    Structural Basis for SARS-CoV-2 Envelope Protein PROTEIN in Recognition of Human Cell Junction Protein PALS1

    Authors: Jin Chai; Yuanheng Cai; Changxu Pang; Liguo Wang; Sean McSweeney; John Shanklin; Qun Liu

    doi:10.1101/2021.02.22.432373 Date: 2021-02-23 Source: bioRxiv

    The COVID-19 pandemic MESHD caused by the SARS-CoV-2 virus has created a global health and economic emergency. SARS-CoV-2 viruses hijack human proteins to promote their spread and virulence including the interactions involving the viral envelope (E) protein PROTEIN and human proteins. To understand the structural basis for SARS-CoV-2 viral-host recognition, we used cryo-electron microscopy to determine a structure for the human cell junction protein PALS1 HGNC and SARS-CoV-2 E protein PROTEIN complex. The structure shows that the E protein PROTEIN C-terminal DLLV motif recognizes a pocket formed exclusively by hydrophobic residues from the PDZ and SH3 domains in PALS1 HGNC. Our structural analysis provides an explanation for the observation that the viral E protein PROTEIN recruits PALS1 HGNC from lung epithelial cell junctions resulting in vascular leakage, lung damage MESHD, viral spread, and virulence. In addition, our structure provides novel targets for peptide- and small-molecule inhibitors that could block the PALS1 HGNC-E interactions to reduce the E-mediated damage to vascular structures.

    SARS-CoV2 Envelope Protein PROTEIN: Non-Synonymous Mutations and Its Consequences

    Authors: Sk Sarif Hassan; Pabitra Pal Choudhury; Bidyut Roy

    id:10.20944/preprints202006.0072.v1 Date: 2020-06-07 Source: Preprints.org

    In the NCBI database, as on June 6, 2020, total number of available complete genome sequences of SARS-CoV2 across the world is 3617. The envelope protein PROTEIN of SARS-CoV2 possesses several non-synonymous mutations over the transmembrane domain and (C)-terminus in 0.414\% of these 3617 genomes. The C-terminus motif DLLV has been changed to DFLV and YLLV in the proteins QJR88103 (Australia: Victoria) and QKI36831 (China: Guangzhou) respectively, which might affect the binding of this motif with the host protein PALS1 HGNC.

    Enhanced binding of SARS-CoV-2 Envelope protein PROTEIN to tight junction-associated PALS1 HGNC could play a key role in COVID-19 MESHD pathogenesis

    Authors: Flavio De Maio; Ettore Lo Cascio; Gabriele Babini; Michela Sali; Stefano Della Longa; Bruno Tilocca; Paola Roncada; Alessandro Arcovito; Maurizio Sanguinetti; Giovanni Scambia; Andrea Urbani

    doi:10.21203/rs.3.rs-30903/v1 Date: 2020-05-21 Source: ResearchSquare

    Background: The Envelope (E) protein PROTEIN of SARS-CoV-2 is the most enigmatic protein among the four structural ones on the viral genome. Most of the current knowledge on the E protein PROTEIN is based on the direct comparison to the SARS E protein PROTEIN, initially mistakenly undervalued and subsequently proved to be a key factor in the ER-Golgi localization and in tight junction disruption. Methods: We compared the genomic sequences of E protein PROTEIN of SARS-CoV-2, SARS-CoV MESHD and the closely related genomes of bats and pangolins obtained from the GISAID and GenBank databases. Multiple sequence alignments were done with the Geneious software using the MAFFT algorithm. In silico modelling analyses of E proteins PROTEIN conformation and docking with PALS1 HGNC were performed with the Schrodinger Suite.Results: When compared to the known SARS E protein PROTEIN, we observed a different amino acidic sequence in the C-terminal of SARS-CoV-2 E protein PROTEIN which might have a key role in the current COVID-19 MESHD pathogenesis. In silico docking results provide evidence of a strengthened binding of SARS-CoV-2 E protein PROTEIN with the tight junction-associated PALS1 HGNC protein.Conclusions: We suggest that SARS-CoV-2 E protein PROTEIN may interfere with the tight junction stability and formation leading to an enhanced epithelial barrier disruption, amplifying the inflammatory processes, and promoting tissue remodelling. These findings raise a warning on the underestimated role of the E protein PROTEIN in the pathogenic mechanism and could open the route to detailed experimental investigations. 

The ZB MED preprint Viewer preVIEW includes all COVID-19 related preprints from medRxiv and bioRxiv, from ChemRxiv, from ResearchSquare, from arXiv and from Preprints.org and is updated on a daily basis (7am CET/CEST).
The web page can also be accessed via API.

Sources


Annotations

All
None
MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins


Export subcorpus as...

This service is developed in the project nfdi4health task force covid-19 which is a part of nfdi4health.

nfdi4health is one of the funded consortia of the National Research Data Infrastructure programme of the DFG.