scholarly journals COVID-19: Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Carbon Dioxide ◽  
Rna Virus ◽  
Host Cells ◽  
Surface Glycoprotein ◽  
The Novel ◽  
Beta Chain ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Bat Coronavirus

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively. At the same time, orf1ab, ORF10, and ORF3a proteins could coordinate attack the heme on the 1-beta chain of hemoglobin to dissociate the iron to form the porphyrin. The attack will cause less and less hemoglobin that can carry oxygen and carbon dioxide. The lung cells have extremely intense poisoning and inflammatory due to the inability to exchange carbon dioxide and oxygen frequently, which eventually results in ground-glass-like lung images. The mechanism also interfered with the normal heme anabolic pathway of the human body, is expected to result in human disease. According to the validation analysis of these finds, chloroquine could prevent orf1ab, ORF3a, and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent, effectively relieve the symptoms of respiratory distress. Since the ability of chloroquine to inhibit structural proteins is not particularly obvious, the therapeutic effect on different people may be different. Favipiravir could inhibit the envelope protein and ORF7a protein bind to porphyrin, prevent the virus from entering host cells, and catching free porphyrins. This paper is only for academic discussion, the correctness needs to be confirmed by other laboratories. Due to the side effects and allergic reactions of drugs such as chloroquine, please consult a qualified doctor for treatment details, and do not take the medicine yourself.</p>

scholarly journals COVID-19: Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Carbon Dioxide ◽  
Rna Virus ◽  
Host Cells ◽  
Surface Glycoprotein ◽  
The Novel ◽  
Beta Chain ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Bat Coronavirus

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively. At the same time, orf1ab, ORF10, and ORF3a proteins could coordinate attack the heme on the 1-beta chain of hemoglobin to dissociate the iron to form the porphyrin. The attack will cause less and less hemoglobin that can carry oxygen and carbon dioxide. The lung cells have extremely intense poisoning and inflammatory due to the inability to exchange carbon dioxide and oxygen frequently, which eventually results in ground-glass-like lung images. The mechanism also interfered with the normal heme anabolic pathway of the human body, is expected to result in human disease. According to the validation analysis of these finds, chloroquine could prevent orf1ab, ORF3a, and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent, effectively relieve the symptoms of respiratory distress. Favipiravir could inhibit the envelope protein and ORF7a protein bind to porphyrin, prevent the virus from entering host cells, and catching free porphyrins. Because the novel coronavirus is dependent on porphyrins, it may originate from an ancient virus. Therefore, this research is of high value to contemporary biological experiments, disease prevention, and clinical treatment.<br></p>

scholarly journals COVID-19: Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Carbon Dioxide ◽  
Rna Virus ◽  
Host Cells ◽  
Surface Glycoprotein ◽  
The Novel ◽  
Beta Chain ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Bat Coronavirus

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively. At the same time, orf1ab, ORF10, and ORF3a proteins could coordinate attack the heme on the 1-beta chain of hemoglobin to dissociate the iron to form the porphyrin. The attack will cause less and less hemoglobin that can carry oxygen and carbon dioxide. The lung cells have extremely intense poisoning and inflammatory due to the inability to exchange carbon dioxide and oxygen frequently, which eventually results in ground-glass-like lung images. The mechanism also interfered with the normal heme anabolic pathway of the human body, is expected to result in human disease. According to the validation analysis of these finds, chloroquine could prevent orf1ab, ORF3a, and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent, effectively relieve the symptoms of respiratory distress. Favipiravir could inhibit the envelope protein and ORF7a protein bind to porphyrin, prevent the virus from entering host cells, and catching free porphyrins. Because the novel coronavirus is dependent on porphyrins, it may originate from an ancient virus. Therefore, this research is of high value to contemporary biological experiments, disease prevention, and clinical treatment.<br></p>

scholarly journals COVID-19: Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Carbon Dioxide ◽  
Rna Virus ◽  
Host Cells ◽  
Surface Glycoprotein ◽  
The Novel ◽  
Beta Chain ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Bat Coronavirus

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively. At the same time, orf1ab, ORF10, and ORF3a proteins could coordinate attack the heme on the 1-beta chain of hemoglobin to dissociate the iron to form the porphyrin. The attack will cause less and less hemoglobin that can carry oxygen and carbon dioxide. The lung cells have extremely intense poisoning and inflammatory due to the inability to exchange carbon dioxide and oxygen frequently, which eventually results in ground-glass-like lung images. The mechanism also interfered with the normal heme anabolic pathway of the human body, is expected to result in human disease. According to the validation analysis of these finds, chloroquine could prevent orf1ab, ORF3a, and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent, effectively relieve the symptoms of respiratory distress. Since the ability of chloroquine to inhibit structural proteins is not particularly obvious, the therapeutic effect on different people may be different. Favipiravir could inhibit the envelope protein and ORF7a protein bind to porphyrin, prevent the virus from entering host cells, and catching free porphyrins. This paper is only for academic discussion, the correctness needs to be confirmed by other laboratories. Due to the side effects and allergic reactions of drugs such as chloroquine, please consult a qualified doctor for treatment details, and do not take the medicine yourself.</p>

scholarly journals COVID-19 Disease: ORF8 and Surface Glycoprotein Inhibit Heme Metabolism by Binding to Porphyrin

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Rna Virus ◽  
Surface Glycoprotein ◽  
The Novel ◽  
Scientific Significance ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Bat Coronavirus ◽  
Anabolic Pathway

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. Due to the limits of the existing experimental tools, many protein roles of novel coronavirus including ORF8 are still unclear. Therefore, in the current scene of an emergency epidemic, it is of high scientific significance to predict the biological role of viral proteins through bioinformatics methods. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively, while orf1ab, ORF10 and ORF3a proteins could coordinately attack heme to dissociate the iron to form the porphyrin. The mechanism seriously interfered with the normal heme anabolic pathway of the human body, being expected to result in human disease. According to the validation analysis of these finds, Chloroquine could prevent orf1ab, ORF3a and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent. Therefore, this research is of high value to contemporary biological experiments, disease prevention and clinical treatment.</p>

scholarly journals COVID-19 Disease: ORF8 and Surface Glycoprotein Inhibit Heme Metabolism by Binding to Porphyrin

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Rna Virus ◽  
Surface Glycoprotein ◽  
The Novel ◽  
Scientific Significance ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Bat Coronavirus ◽  
Anabolic Pathway

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. Due to the limits of the existing experimental tools, many protein roles of novel coronavirus including ORF8 are still unclear. Therefore, in the current scene of an emergency epidemic, it is of high scientific significance to predict the biological role of viral proteins through bioinformatics methods. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively, while orf1ab, ORF10 and ORF3a proteins could coordinately attack heme to dissociate the iron to form the porphyrin. The mechanism seriously interfered with the normal heme anabolic pathway of the human body, being expected to result in human disease. According to the validation analysis of these finds, Chloroquine could prevent orf1ab, ORF3a and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent. Therefore, this research is of high value to contemporary biological experiments, disease prevention and clinical treatment.</p>

scholarly journals COVID-19 Disease: ORF8 and Surface Glycoprotein Inhibit Heme Metabolism by Binding to Porphyrin

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Rna Virus ◽  
Surface Glycoprotein ◽  
The Novel ◽  
Scientific Significance ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Bat Coronavirus ◽  
Anabolic Pathway

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory infection caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. Due to the limits of the existing experimental tools, many protein roles of novel coronavirus including ORF8 are still unclear. Therefore, in the current scene of an emergency epidemic, it is of high scientific significance to predict the biological role of viral proteins through bioinformatics methods. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of certain proteins of the novel coronavirus. The results showed the ORF8 and surface glycoprotein could bind to the porphyrin, respectively, while orf1ab, ORF10 and ORF3a proteins could coordinately attack heme to dissociate the iron to form the porphyrin. The mechanism seriously interfered with the normal heme anabolic pathway of the human body, being expected to result in human disease. According to the validation analysis of these finds, Chloroquine could prevent orf1ab, ORF3a and ORF10 to attack the heme to form the porphyrin, and inhibit the binding of ORF8 and surface glycoproteins to porphyrins to a certain extent. Therefore, this research is of high value to contemporary biological experiments, disease prevention and clinical treatment.</p>

scholarly journals COVID-19:Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

2020 ◽  
Author(s):  
liu wenzhong ◽  
Li hualan
Keyword(s):  
Rna Virus ◽  
The Novel ◽  
Beta Chain ◽  
Nonstructural Proteins ◽  
Efficacy Analysis ◽  
Treatment Information ◽  
Specific Proteins ◽  
Positive Strand Rna Virus ◽  
Novel Coronavirus ◽  
Positive Strand Rna

<p>The novel coronavirus pneumonia (COVID-19) is an infectious acute respiratory caused by the novel coronavirus. The virus is a positive-strand RNA virus with high homology to bat coronavirus. In this study, conserved domain analysis, homology modeling, and molecular docking were used to compare the biological roles of specific proteins of the novel coronavirus. The results showed that some viral structural and nonstructural proteins could bind to the porphyrin, respectively. At the same time, orf1ab, ORF10 and ORF3a proteins coordinated to attack heme on the 1-beta chain of hemoglobin, dissociating iron to form porphyrin. Deoxyhemoglobin is more vulnerable to virus attacks than oxidized hemoglobin. The attack will cause less and less hemoglobin that can carry oxygen and carbon dioxide, producing symptoms of respiratory distress. Virus attack damaged many organs and tissues. Lung cells are toxic and inflammatory due to derivatives produced by the attack, which eventually resulted in ground-glass-like lung images. Capillaries easily broken due to inflammation. Proteins such as fibrinogen filled the capillaries' cracks through the coagulation reaction. Therefore, many fibrin and thrombus gathered in the lung tissue of critically ill patients. The mechanism also interfered with the normal heme anabolic pathway of the human body, expecting to result in human disease. This paper is only for academic discussion, the correctness of the theory needs to be confirmed by other experiments. According to the reader's suggestion, the content of the drug-related efficacy analysis has been deleted. Due to the side effects of drugs, please consult a qualified doctor for detailed treatment information, and do not take the drug yourself. We look forward to these discoveries bringing more ideas to people and inspiring people's confidence in defeating the virus.</p>

scholarly journals SARS-CoV-2 Isolation and Propagation from Turkish COVID-19 patients

2020 ◽  
Author(s):  
Cihan Tastan ◽  
Bulut Yurtsever ◽  
Gozde Sir ◽  
Derya Dilek Kancagi ◽  
Sevda Demir ◽  
...  
Keyword(s):  
Rna Virus ◽  
The Novel ◽  
Isolation And Characterization ◽  
Characterization Studies ◽  
Positive Strand Rna Virus ◽  
The Republic ◽  
Novel Coronavirus ◽  
Positive Strand Rna ◽  
Vaccine Testing ◽  
Republic Of Turkey

AbstractThe novel coronavirus pneumonia, which was named later as Coronavirus Disease 2019 (COVID-19), is caused by the Severe Acute Respiratory Syndrome Coronavirus 2, namely SARS-CoV-2. It is a positive-strand RNA virus that is the seventh coronavirus known to infect humans. The COVID-19 outbreak presents enormous challenges for global health behind the pandemic outbreak. The first diagnosed patient in Turkey has been reported by the Republic of Turkey Ministry of Health on March 11, 2020. Today, over ninety thousand cases in Turkey, and two million cases around the world have been declared. Due to the urgent need for vaccine and anti-viral drug, isolation of the virus is crucial. Here, we report one of the first isolation and characterization studies of SARS-CoV-2 from nasopharyngeal and oropharyngeal specimens of diagnosed patients in Turkey. This study provides an isolation and replication methodology, and cell culture tropism of the virus that will be available to the research communities.Article SummaryScientists have isolated virus from Turkish COVID-19 patients. The isolation, propagation, and plaque and immune response assays of the virus described here will serve in following drug discovery and vaccine testing.

Increase of SARS-CoV 3CL peptidase activity due to macromolecular crowding effects in the milieu composition

2010 ◽  
Vol 391 (12) ◽  
Author(s):  
Debora N. Okamoto ◽  
Lilian C.G. Oliveira ◽  
Marcia Y. Kondo ◽  
Maria H.S. Cezari ◽  
Zoltán Szeltner ◽  
...  
Keyword(s):  
Rna Virus ◽  
Antiviral Agents ◽  
Fine Tuning ◽  
Host Cells ◽  
Respiratory Syndrome Virus ◽  
Peptidase Activity ◽  
Buffer Solutions ◽  
Tuning Mechanism ◽  
Positive Strand Rna Virus ◽  
Positive Strand Rna

Abstract The 3C-like peptidase of the severe acute respiratory syndrome virus (SARS-CoV) is strictly required for viral replication, thus being a potential target for the development of antiviral agents. In contrast to monomeric picornavirus 3C peptidases, SARS-CoV 3CLpro exists in equilibrium between the monomer and dimer forms in solution, and only the dimer is proteolytically active in dilute buffer solutions. In this study, the increase of SARS-CoV 3CLpro peptidase activity in presence of kosmotropic salts and crowding agents is described. The activation followed the Hofmeister series of anions, with two orders of magnitude enhancement in the presence of Na2SO4, whereas the crowding agents polyethylene glycol and bovine serum albumin increased the hydrolytic rate up to 3 times. Kinetic determinations of the monomer dimer dissociation constant (K d) indicated that activation was a result of a more active dimer, without significant changes in K d values. The activation was found to be independent of substrate length and was derived from both k cat increase and K m decrease. The viral peptidase activation described here could be related to the crowded intracellular environment and indicates a further fine-tuning mechanism for biological control, particularly in the microenvironment of the vesicles that are induced in host cells during positive strand RNA virus infection.

scholarly journals The landscape of SARS-CoV-2 RNA modifications

2020 ◽  
Author(s):  
Milad Miladi ◽  
Jonas Fuchs ◽  
Wolfgang Maier ◽  
Sebastian Weigang ◽  
Núria Díaz i Pedrosa ◽  
...  
Keyword(s):  
Host Cell ◽  
Rna Virus ◽  
Open Reading Frames ◽  
Lung Epithelial Cells ◽  
Host Cells ◽  
Rna Modification ◽  
Rna Modifications ◽  
Positive Strand Rna Virus ◽  
Novel Therapeutic Strategies ◽  
Positive Strand Rna

AbstractIn 2019 the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) caused the first documented cases of severe lung disease COVID-19. Since then, SARS-CoV-2 has been spreading around the globe resulting in a severe pandemic with over 500.000 fatalities and large economical and social disruptions in human societies. Gaining knowledge on how SARS-Cov-2 interacts with its host cells and causes COVID-19 is crucial for the intervention of novel therapeutic strategies. SARS-CoV-2, like other coronaviruses, is a positive-strand RNA virus. The viral RNA is modified by RNA-modifying enzymes provided by the host cell. Direct RNA sequencing (DRS) using nanopores enables unbiased sensing of canonical and modified RNA bases of the viral transcripts. In this work, we used DRS to precisely annotate the open reading frames and the landscape of SARS-CoV-2 RNA modifications. We provide the first DRS data of SARS-CoV-2 in infected human lung epithelial cells. From sequencing three isolates, we derive a robust identification of SARS-CoV-2 modification sites within a physiologically relevant host cell type. A comparison of our data with the DRS data from a previous SARS-CoV-2 isolate, both raised in monkey renal cells, reveals consistent RNA modifications across the viral genome. Conservation of the RNA modification pattern during progression of the current pandemic suggests that this pattern is likely essential for the life cycle of SARS-CoV-2 and represents a possible target for drug interventions.

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