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SARS-CoV-2 proteins

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    Successful Remote Monitoring During COVID-19 Pandemic MESHD of Patients with Inborn Errors of the Amino acid Metabolism MESHD not including PKU MESHD from a Single Reference center using Filter Paper Samples

    Authors: Sinziana Stanescu; Amaya Belanger-Quintana; Francisco Arrieta; Patricia Alcaide; Pedro Ruiz-Sala

    doi:10.21203/rs.3.rs-122663/v1 Date: 2020-12-05 Source: ResearchSquare

    Background. Patients with inborn errors of metabolism MESHD ( IEM MESHD) pose specific management challenges, considering their multisystem involvement. Among them, children and adults with organic acidemias MESHD ( OA MESHD) and other disorders of the amino acid metabolism have a high risk for severe metabolic events that need to be recognized and promptly treated, and therefore require frequent clinical and biochemical evaluations. The novel highly pathogenic SARS-CoV2 virus appeared in Europe in the first trimester of 2020. This pandemic has a huge impact on the health care systems all over the world, interrupting the follow-up of many chronic diseases MESHD. For metabolic patients, travel to reference units may be reduced due to mobility restrictions but more importantly, attendance to medical facilities can be a risk of infection that can be a danger in itself but also trigger a metabolic decompensation.Methods. During the first coronavirus disease ( COVID-19 MESHD) outbreak in Spain from March to June 2020, we designed a model of remote monitoring of our patients with amino acid disorders using telephone and/or online clinical assessments and using filter paper samples to continue the biochemical control. Results. Fourteen patients with inborn errors of amino acid metabolism MESHD other than PKU MESHD received filter papers and instructions to collect blood and urine samples home and send them to our reference laboratory. Conclusions. Considering the COVID19 MESHD pandemic evolution, new strategies to ensure IEM MESHD patients have an evaluation continuity need to be implemented. We believe that blood and urine filter paper biochemical follow-up, together with online or telephone clinical assessments, can help minimize the need for in-hospital visits. 

    Single Amino Acid Variant (SAV) Percentage and Monomer Modeling of Spike Protein PROTEIN of SARS-CoV-2 in Jordan

    Authors: Walid Al-Zyoud; Hazem Haddad; Ramzi Foudeh

    id:10.20944/preprints202006.0184.v1 Date: 2020-06-14 Source: Preprints.org

    Spike protein PROTEIN is the surface glycoprotein of the severe acute respiratory syndrome-coronavirus-2 MESHD (SARS-CoV-2) necessary for the entry of the virus via the transmembrane receptors of the human endothelial cells of the respiratoty system for the virus to be engulfed causing COVID-19 MESHD disease after priming by type II transmembrane protease TMPRSS2 HGNC and then binding with the angiotensin-converting enzyme 2 HGNC ( ACE2 HGNC). Therefore, mutations and amino acid variants analysis are essential in understanding the mechanism of binding of spike protein PROTEIN with its receptor to have an insights on possibilities to design a peptide or nucleotide-based vaccine for COVID-19 MESHD. Here, we employed Iterative Threading Assembly Refinement (I-TASSER) and Multiple Alignment using Fast Fourier Transform (MAFFT) to predict the three-dimensional monomer structure of spike protein PROTEIN of SARS-CoV-2 and to analyze the amino acid variants for protein sequences from GISAID database for samples collected from Jordan in a try to find an explanation for the low confirmed number of COVID-19 MESHD in Jordan. Our Protein Homology/analogY Recognition Engine V 2.0 (Phyre2) findings showed four single amino acid variants ( SAV MESHD) found in 20 samples of SARS-CoV-2. What is equal to 5% of samples showed tyrosine deletion at Y144 located in the SARS-CoV-like_Spike_S1_NTD (N terminal domain), 62% showed aspartate substitution to glycine at D614G located in the SARS-CoV-2_Spike_S1_RBD (spike recognition binding site), 5% showed aspartate substitution to tyrosine at D1139Y and 5% showed glycine substitution to serine at G1167S both located in the Corona_S2 domain. The findings have shown lower mutational sensitivity in all variants that might not affect the function of spike glycoprotein PROTEIN except for D614G, which has the highest mutational sensitivity score (5 out of 9) indicating a higher likelihood to affect the function of the spike protein PROTEIN. This might suggest, in general, a reduced transmitability of SARS-CoV-2 in Jordan.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins


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