چاپ صفحه |  صفحه نخست سامانه |  نویسندگان |  اطلاعات تفضیلی |  دانلود مقاله | دانشگاه علوم پزشکی تبریز |
| نویسنده ثبت کننده مقاله | وحدت پورطهماسبی |
| مرحله جاری مقاله | تایید نهایی |
| دانشکده/مرکز مربوطه | بیماری های عفونی و گرمسیری |
| کد مقاله | 80299 |
| عنوان فارسی مقاله | Mutational and structural analysis of SARS-CoV-2 envelope proteins among iranian COVID-19 positive patients |
| عنوان لاتین مقاله | Mutational and structural analysis of SARS-CoV-2 envelope proteins among iranian COVID-19 positive patients |
| نوع ارائه | پوسترو سخنرانی |
| عنوان کنگره / همایش | 32nd European Congress of Clinical Microbiology & Infectious Diseases (ECCMID) |
| نوع کنگره / همایش | بین المللی |
| کشور محل برگزاری کنگره/ همایش | Portugal |
| شهر محل برگزاری کنگره/ همایش | Lisbon |
| سال انتشار/ ارائه شمسی | 1401 |
| سال انتشار/ارائه میلادی | 2022 |
| تاریخ شمسی شروع و خاتمه کنگره/همایش | 1401/02/03 الی 1401/09/06 |
| آدرس لینک مقاله/ همایش در شبکه اینترنت | https://markterfolg.de/ESCMID/Final_Programme_2022/#page=1 |
| آدرس علمی (Affiliation) نویسنده متقاضی | Infectious and Tropical Diseases Research Center, Tabriz University of Medical Sciences, Tabriz, Iran |
| نویسنده | نفر چندم مقاله |
|---|---|
| مریم عاجل | اول |
| مهین آهنگر اسکوئی | دوم |
| حسین بنازاده باغی | سوم |
| آلکا حسنی | چهارم |
| مجتبی ورشوچی فرد | ششم |
| وحدت پورطهماسبی | هفتم |
| عنوان | متن |
|---|---|
| خلاصه مقاله | Background SARS-CoV-2 envelope protein is an integral membrane protein mainly found in the Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC) and has 75 amino acids. This protein is important for viral entry, assembly, and budding. The DLLV motif of envelope protein binds to the host cell PALS1 protein to facilitate infection. The aims of this study were to find out the prevalence of mutations) in envelope proteins of SARS-CoV-2, as well as to analyze the three-dimensional (3D) properties of envelope mutant in COVID-19 patients. Methods One hundred Iranian COVID-19 patients infected with SARS-CoV-2 alpha variants (n= 40), beta variants (n= 30) and delta variants (n= 30) were enrolled in this study. SARS-CoV-2 RNA was extracted from samples. Finally, the RNA was eluted using 50 μL of elution buffer and stored at -20 °C. The envelope genes from 90 patients were amplified and directly sequenced. The sequences were analyzed using Chromas and BioEdit software. The 3D structure of SARS-CoV-2 envelope protein for both the wild-type (Accession number: YP_009724392) and mutants were evaluated using several web tools. The immunogenic activity of the wild-type and mutant envelope was also analyzed using a docking server. Results Direct sequencing data from 100 available sequences was indicated that only, 2 samples contained mutation in envelope protein (L73F and S68F) (Figure 1). Also, stretch of silent mutation were found in envelope genes. The 3D features of individual aminoacid mutations and their potential impacts on 3D structure of ‘envelope mutants were also determined. The mutations also increased the stability of the envelope protein. Molecular docking showed that the mutation caused an alteration binding affinity between the envelope and cellular protein PALS-1 (Protein Associated with Caenorhabditis elegans Lin-7 protein 1). 03405 Mutational and Structural Analysis of SARS-CoV-2 Envelope Proteins Among Iranian COVID-19 Positive Patients Conclusions SARS-CoV-2 envelope gene observed to be conserved in the majority of COVID-19 patients. Mutations in SARS-CoV-2 indicating a more stabilizing effect. Effective antiviral drugs, and vaccines may be designed after evaluation the envelope gene variations for better prevention and treatment of SARS-CoV-2 infection. |
| کلمات کلیدی | SARS-CoV-2, Envelope, Mutation |
| نام فایل | تاریخ درج فایل | اندازه فایل | دانلود |
|---|---|---|---|
| SARS-CoV-2 Certificate.pdf | 1401/09/05 | 275135 | دانلود |
| Abstract SARS-CoV-2.pdf | 1401/09/05 | 138838 | دانلود |
