Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinS (2)


SARS-CoV-2 Proteins
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    ACE2 HGNC Homo-dimerization, Human Genomic variants and Interaction of Host Proteins Explain High Population Specific Differences in Outcomes of COVID19 MESHD

    Authors: Swarkar Sharma; Inderpal Singh; Shazia Haider; Md. Zubbair Malik; Kalaiarasan Ponnusamy; Ekta Rai

    doi:10.1101/2020.04.24.050534 Date: 2020-04-24 Source: bioRxiv

    Severe acute respiratory syndrome coronavirus 2 MESHD (SARS-CoV-2) is a positive single-stranded RNA virus that causes a highly contagious Corona Virus Disease MESHD ( COVID19 MESHD). Entry of SARS-CoV-2 in human cells depends on binding of the viral spike (S) proteins PROTEIN to cellular receptor Angiotensin-converting enzyme 2 ( ACE2 HGNC) and on S-protein PROTEIN S-protein HGNC priming by host cell serine protease TMPRSS2 HGNC. Recently, COVID19 MESHD has been declared pandemic by World Health Organization (WHO) yet high differences in disease outcomes across countries have been seen. We provide evidences to explain these population-level differences. One of the key factors of entry of the virus in host cells presumably is because of differential interaction of viral proteins with host cell proteins due to different genetic backgrounds. Based on our findings, we conclude that a higher expression of ACE2 HGNC is facilitated by natural variations, acting as Expression quantitative trait loci (eQTLs), with different frequencies in different populations. We suggest that high expression of ACE2 HGNC results in homo-dimerization, proving disadvantageous for TMPRSS2 HGNC mediated cleavage of ACE2 HGNC; whereas, the monomeric ACE2 HGNC has higher preferential binding with SARS-CoV-2 S-Protein vis MESHD S-Protein PROTEIN S-Protein HGNC vis-a-vis its dimerized counterpart. Further, eQTLs in TMPRSS2 HGNC and natural structural variations in the gene may also result in differential outcomes towards priming of viral S-protein HGNC S-protein PROTEIN, a critical step for entry of the Virus in host cells. In addition, we suggest that several key host genes, like SLC6A19 HGNC, ADAM17 HGNC, RPS6 HGNC, HNRNPA1 HGNC, SUMO1 HGNC, NACA HGNC, BTF3 HGNC and some other proteases as Cathepsins, might have a critical role. To conclude, understanding population specific differences in these genes may help in developing appropriate management strategies for COVID19 MESHD with better therapeutic interventions.

    Structural basis for the recognition of the 2019-nCoV by human ACE2

    Authors: Renhong Yan; Yuanyuan Zhang; Yingying Guo; Lu Xia; Qiang Zhou

    doi:10.1101/2020.02.19.956946 Date: 2020-02-20 Source: bioRxiv

    Angiotensin-converting enzyme 2 HGNC ( ACE2 HGNC) has been suggested to be the cellular receptor for the new coronavirus (2019-nCoV) that is causing the coronavirus disease 2019 MESHD ( COVID-19 MESHD). Like other coronaviruses such as the SARS-CoV, the 2019-nCoV uses the receptor binding domain (RBD) of the surface spike glycoprotein PROTEIN ( S protein PROTEIN S protein HGNC) to engage ACE2 HGNC. We most recently determined the structure of the full-length human ACE2 HGNC in complex with a neutral amino acid transporter B0AT1 HGNC. Here we report the cryo-EM structure of the full-length human ACE2 HGNC bound to the RBD of the 2019-nCoV at an overall resolution of 2.9 [A] in the presence of B0AT1 HGNC. The local resolution at the ACE2 HGNC-RBD interface is 3.5 [A], allowing analysis of the detailed interactions between the RBD and the receptor. Similar to that for the SARS-CoV MESHD, the RBD of the 2019-nCoV is recognized by the extracellular peptidase domain (PD) of ACE2 HGNC mainly through polar residues. Pairwise comparison reveals a number of variations that may determine the different affinities between ACE2 HGNC and the RBDs from these two related viruses.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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