ABSTRACT
On March 11, 2020, the World Health Organization (WHO) declared a new coronavirus infection caused by the SARS-CoV-2 virus as a pandemic, making it the 11th pandemic of the 20th and 21st centuries. This study investigated the clinical and laboratory results (D-dimer, conventional coagulation, and HbA1c biomarker concentrations) of 150 patients (75 male and 75 female) with confirmed COVID-19 pneumonia and 50 controls (25 male and 25 female). For disease diagnosis, all COVID-19 patients were given a Real-Time Reverse Transcription Polymerase Chain Reaction Assay (RT-PCR). The findings revealed that D-dimer and HbA1c levels in COVID-19 patients were significantly higher (P 0.001) at the time of admission; In COVID-19 patients, there was also a strong correlation between D-dimer levels and HbA1c levels (P 0.001). In conclusion, COVID-19 patients are more likely to have a poor prognosis if their D-dimer and HbA1c levels remain uncontrolled over a lengthy period. To lower the likelihood of a bad prognosis in COVID-19, patients with higher levels of D-dimer and HbA1c should be continuously monitored.
Subject(s)
COVID-19 , Humans , Male , Female , COVID-19/diagnosis , SARS-CoV-2 , Glycated Hemoglobin , IraqABSTRACT
The world today is battling with a coronavirus infection that is considered a global pandemic. Coronavirus infection is mainly attribute to the varying technique of the replication and release of different genomic components of the virus. The present study aims to establish the physical and chemical features, as well as the basic structural and functional properties of Coronavirus ORF1ab domain. A molecular approach was adopt in this study using the Swiss Model and Phyre2 server whereas the prediction of the active ligand binding sites was done using Phyre2. The analysis of the structure of the protein showed that it has good structural and heat stability, as well as better hydrophilic features and acidic in nature. Based on the Homology modeling, only two binding active sites were noted with catalytic function being mediated by Zn2+ as the metallic heterogeneous ligand for binding sites prediction. The proteins mostly exhibited helical secondary configurations. This study can help in predicting and understanding the role of this domain protein in active coronavirus infection.
ABSTRACT
The world today is battling with a coronavirus infection which is considered a global pandemic. Coronavirus infection is mainly attributed to the varying technique of the replication and releaseof different genomic components of the virus. In this study, the aim is to establish the physical and chemical features, as well as the basic structural and functional properties of Coronavirus ORF1ab domain. A molecular approach was adopted in this study using the Swiss Model & Phyre2 server while the prediction of the active ligand binding sites was done using Phyre2.The analysis of the structure of the protein showed that it has good structural and heat stability, as well as better hydrophilic features and acidic in nature. Based on the Homology modelling, only 2 binding active sites were noted with catalytic function being mediated by Zn2+ as the metallic heterogen ligand for binding sites prediction. The proteins mostly exhibited helical secondary configurations. This study can help in predicting and understanding the role of this domain protein in active coronavirus infection.