Corpus overview


MeSH Disease

Human Phenotype


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    Genetic Uniformity of a Specific Region in SARS-CoV-2 Genome and In-Silico Target-Oriented Repurposing of N-Acetyl-D-Glucosamine

    Authors: Omur Baysal; Ragip Soner Silme; Cagatay Karaaslan

    id:10.20944/preprints202005.0397.v1 Date: 2020-05-24 Source:

    Causative agent of the viral pneumonia MESHD pneumonia HP outbreak in the World identified as SARS-CoV2 leads to a severe respiratory illness like SARS and MERS. The pathogen spreading has turned into a pandemic dissemination and increased the mortality rate. Therefore, useful information is urgently necessary for effective control of the disease MESHD. Our study shows the existence of unvarying sequence with no mutation, including ORF1ab regions in 134 high-quality filtered genome sequences of SARS-CoV2 downloaded from the GISAID database. We have detected this sequence stability by using MAUVE analysis and pairwise alignment with Global Needleman Wunsch algorithm for each two different sequences, reciprocally. They also confirmed all these results were also with the Clustal W analysis. The first 6500 bp including ORF1ab region is an unvarying sequence. According to the highest TM-score of predicted protein structure analysis, the results showed it is very similar to spike protein of feline infectious peritonitis MESHD peritonitis HP virus strain UU4 (PDB 6JX7) depending on amino acid sequences encoded by this unvarying region, and N-acetyl-D-glucosamine is the ligand of this protein. These results have confirmed that N-acetyl-D-glucosamine could play an important role in controlling of SARS-CoV-2. Also, our molecular docking analysis data supports a strong protein-ligand interaction of N-acetyl-D-glucosamine with spike receptor-binding domain bound with ACE2 (PDB 6M0J) and RNA-binding domain of nucleocapsid phosphoprotein (PDB 6WKP) from SARS CoV-2. Therefore, binding of N-acetyl-D-glucosamine to these proteins could inhibit SARS CoV-2’s replication. In the present work, we have suggested providing a repurposing compound for further in vitro and in vivo studies and new insights for ongoing clinical treatments as a new strategy to control of SARS-CoV-2 infections MESHD.

    Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication

    Authors: Wayne Vuong; Muhammad Bashir Khan; Conrad Fischer; Elena Arutyunova; Tess Lamer; Justin Shields; Holly A Saffran; Ryan T McKay; Marco J van Belkum; Michael Joyce; Howard S Young; D. Lorne Tyrrell; John C Vederas; M Joanne Lemieux

    doi:10.1101/2020.05.03.073080 Date: 2020-05-04 Source: bioRxiv

    The COVID-19 pandemic, attributed to the SARS-CoV-2 coronavirus infection MESHD, resulted in millions infected worldwide and an immediate need for antiviral treatments. The main protease (Mpro) in SARS-CoV-2 is a viable drug target because of its essential role in the cleavage of the virus polypeptide and subsequent viral replication. Feline infectious peritonitis MESHD peritonitis HP, a fatal infection MESHD in cats caused by a coronavirus, was successfully treated previously with a dipeptide-based protease inhibitor. Here we show this drug, GC376, and its analog GC373, are effective inhibitors of the Mpro from both SARS-CoV and SARS-CoV-2 with IC50 values in the nanomolar range. Crystal structures of the SARS-CoV and SARS-CoV-2 Mpro with these inhibitors have a covalent modification of the nucleophilic Cys145. NMR analysis reveals that inhibition proceeds via reversible formation of a hemithioacetal. GC373 and GC376 are potent inhibitors of SARS-CoV-2 in cell culture, with EC50 values near one micromolar and little to no toxicity. These protease inhibitors are soluble, non-toxic, and bind reversibly. They are strong drug candidates for the treatment of human coronavirus infections MESHD because they have already been successful in animals (cats). The work here lays the framework for their use in human trials for the treatment of COVID-19.

    SARS-CoV-2 neutralizing serum SERO antibodies SERO in cats: a serological investigation

    Authors: Meilin Jin

    doi:10.1101/2020.04.01.021196 Date: 2020-04-03 Source: bioRxiv

    Coronavirus disease MESHD 2019 (COVID-19) caused by severe acute respiratory syndrome MESHD coronavirus 2 (SARS-CoV-2) was first reported in Wuhan, China, and rapidly spread worldwide. Previous studies suggested cat could be a potential susceptible animal of SARS-CoV-2. Here, we investigated the infection MESHD of SARS-CoV-2 in cats by detecting specific serum SERO antibodies SERO. A cohort of serum samples SERO were collected from cats in Wuhan, including 102 sampled after COVID-19 outbreak, and 39 prior to the outbreak. 15 of 102 (14.7%) cat sera collected after the outbreak were positive for the receptor binding domain (RBD) of SARS-CoV-2 by indirect enzyme linked immunosorbent assay SERO ( ELISA SERO). Among the positive samples, 11 had SARS-CoV-2 neutralizing antibodies SERO with a titer ranging from 1/20 to 1/1080. No serological cross-reactivity was detected between the SARS-CoV-2 and type I or II feline infectious peritonitis MESHD peritonitis HP virus (FIPV). Our data demonstrates that SARS-CoV-2 has infected cat population in Wuhan during the outbreak.

    Feline coronaviruses associated with feline infectious peritonitis MESHD peritonitis HP have modifications to spike protein activation sites at two discrete positions

    Authors: Beth N. Licitra; Kelly L. Sams; Donald W. Lee; Gary R. Whittaker

    id:1412.4034v1 Date: 2014-12-12 Source: arXiv

    Feline infectious peritonitis MESHD peritonitis HP (FIP) is associated with mutations in the feline coronavirus (FCoV) genome that are thought to convert the subclinical feline enteric coronavirus (FECV) into the lethal feline infectious peritonitis MESHD peritonitis HP virus (FIPV). A key feature of FIPV, not shared with FECV, is the productive infection MESHD of macrophages. Therefore mutations in proteins that govern cell tropism, such as the spike glycoprotein, may play an important role in FIP progression. In a prior study, involving a limited number of samples, we have shown an association of FIP with mutations in the protease cleavage-activation site located between the receptor-binding and fusion domains of the FCoV spike (S1/S2). Here, we extend these studies to investigate a larger sample set and to obtain a more refined analysis of the mutations at this S1/S2 site. Our larger data set more clearly shows that the mutations acquired by FIPV at S1/S2 are also accompanied by additional mutations at a second protease cleavage-activation site located in the fusion domain (S2'), adjacent to the viral fusion peptide. Overall, our data indicate a pattern of mutations across the two protease recognition sites that results in substitutions, and/or altered recognition, of critical basic/polar amino acid residues needed for virus activation in the enteric tract. Typically, FIPVs have substitutions of non-polar, aliphatic or aromatic residues in the protease recognition sites. These changes likely modulate the proteolytic activation of the virus and its ability to productively infect macrophages in vivo.

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MeSH Disease
Human Phenotype

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