Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinS (3)


SARS-CoV-2 Proteins
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    A new proposed mechanism of some known drugs targeting the SARS-CoV-2 spike PROTEIN glycoprotein using molecular docking

    Authors: Tarek Moussa; Nevien Sabry

    doi:10.21203/ Date: 2020-11-10 Source: ResearchSquare

    COVID-19 MESHD is caused by the novel enveloped beta-coronavirus with a genomic RNA closely related to severe acute respiratory syndrome-corona virus MESHD ( SARS-CoV MESHD) and is named coronavirus 2 (SARS-CoV-2). The receptor binding domain (RBD) of the S-protein PROTEIN S-protein HGNC interacts with the human ACE-2 HGNC receptor that enables the initiation of viral entry. Hence, blocking the S-protein PROTEIN S-protein HGNC interactions by means of synthetic compounds mark the pivotal step for targeting SARS-CoV-2. Most of the six compounds were observed to fit nicely with specific noncovalent interactions, including H bonds, electrostatic, Van der Waals and hydrophobic bonds (pi and sigma bonds). Oseltamivir was found to be the most strongly interacting with the RBD, exhibiting high values of full fitness MESHD and low free energy of binding. it formed multiple noncovalent bonds in the region of the active site. Hydroxychloroquine also demonstrated high binding affinity in the solvent accessbility state and fit nicely into the active pocket of the S-protein PROTEIN S-protein HGNC. The results revealed that these compounds could be potent inhibitors of S-protein PROTEIN S-protein HGNC that could, to some extent, block its interaction with ACE-2 HGNC. It is obvious from the 3D structure of SARS-CoV-2 spike PROTEIN protein was changed with the interaction of different drugs, which led to the unsuitability to bind ACE2 HGNC receptor. Hence, laboratory studies elucidating the action of these compounds on SARS-CoV-2 are warranted for clinical assessments. Chloroquine, hydroxychloroquine and oseltamivir interacted well with the receptor binding domain of S-protein PROTEIN S-protein HGNC via noncovalent interactions and recommended as excellent candidates for COVID-19 MESHD

    A Multiscale and Comparative Model for Receptor Binding of 2019 Novel Coronavirus and the Implication of its Life Cycle in Host Cells

    Authors: Zhaoqian Su; Yinghao Wu

    doi:10.1101/2020.02.20.958272 Date: 2020-02-21 Source: bioRxiv

    The respiratory syndrome MESHD caused by a new type of coronavirus has been emerging from China and caused more than 1000 death globally since December 2019. This new virus, called 2019 novel coronavirus (2019-nCoV) uses the same receptor called Angiotensinconverting enzyme 2 ( ACE2 HGNC) to attack humans as the coronavirus that caused the severe acute respiratory syndrome MESHD (SARS) seventeen years ago. Both viruses recognize ACE2 HGNC through the spike proteins (S PROTEIN S-protein HGNC) on their surfaces. It was found that the S-protein PROTEIN S-protein HGNC from the SARS coronavirus ( SARS-CoV MESHD) bind stronger to ACE2 HGNC than 2019-nCoV. However, function of a bio-system is often under kinetic, rather than thermodynamic, control. To address this issue, we constructed a structural model for complex formed between ACE2 HGNC and the S-protein PROTEIN S-protein HGNC from 2019-nCoV, so that the rate of their association can be estimated and compared with the binding of S-protein HGNC S-protein PROTEIN from SARS-CoV MESHD by a multiscale simulation method. Our simulation results suggest that the association of new virus to the receptor is slower than SARS, which is consistent with the experimental data obtained very recently. We further integrated this difference of association rate between virus and receptor into a mathematical model which describes the life cycle of virus in host cells and its interplay with the innate immune system. Interestingly, we found that the slower association between virus and receptor can result in longer incubation period, while still maintaining a relatively higher level of viral concentration in human body. Our computational study therefore provides, from the molecular level, one possible explanation that the new disease by far spread much faster than SARS.

    Fast assessment of human receptor-binding capability of 2019 novel coronavirus (2019-nCoV)

    Authors: Qiang Huang; Andreas Herrmann

    doi:10.1101/2020.02.01.930537 Date: 2020-02-03 Source: bioRxiv

    The outbreaks of 2002/2003 SARS, 2012/2015 MERS and 2019/2020 Wuhan respiratory syndrome MESHD clearly indicate that genome evolution of an animal coronavirus (CoV) may enable it to acquire human transmission ability, and thereby to cause serious threats to global public health. It is widely accepted that CoV human transmission is driven by the interactions of its spike protein (S PROTEIN S-protein HGNC) with human receptor on host cell surface; so, quantitative evaluation of these interactions may be used to assess the human transmission capability of CoVs. However, quantitative methods directly using viral genome data are still lacking. Here, we perform large-scale protein-protein docking to quantify the interactions of 2019-nCoV S-protein HGNC S-protein PROTEIN receptor-binding domain (S-RBD) with human receptor ACE2 HGNC, based on experimental SARS-CoV S-RBD MESHD- ACE2 HGNC complex structure. By sampling a large number of thermodynamically probable binding conformations with Monte Carlo algorithm, this approach successfully identified the experimental complex structure as the lowest-energy receptor-binding conformations, and hence established an experiment-based strength reference for evaluating the receptor-binding affinity of 2019-nCoV via comparison with SARS-CoV MESHD. Our results show that this binding affinity is about 73% of that of SARS-CoV MESHD, supporting that 2019-nCoV may cause human transmission similar to that of SARS-CoV MESHD. Thus, this study presents a method for rapidly assessing the human transmission capability of a newly emerged CoV and its mutant strains, and demonstrates that post-genome analysis of protein-protein interactions may provide early scientific guidance for viral prevention and control.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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