{"title":"Comparison of Fragments in Human Hemostatic Proteins That Mimics Fragments in Proteins of A/H1N1 Viruses and Coronaviruses.","authors":"I N Zhilinskaya, V A Marchenko, E P Kharchenko","doi":"10.3103/S0891416822040103","DOIUrl":null,"url":null,"abstract":"<p><p><b>Objective</b>: To compare the repertoire of proteins of the human hemostatic system and fragments mimicking these proteins in the proteins of influenza A/H1N1 viruses and coronaviruses. <b>Material and methods</b>. Influenza viruses A/H1N1 (A/Brevig Mission/1/18), A/St. Petersburg /RII04/2016 (H1N1)pdm09, coronaviruses SARS-CoV and SARS-CoV-2 (strain Wuhan-Hu-1) were used for comparative computer analysis. The sources of the primary structures of proteins of the analyzed viruses and 41 proteins of the human hemostatic system were publicly available Internet databases, respectively, www.ncbi.nlm.nih.gov and www.nextprot.org. The search for homologous sequences in the structure of viral proteins and hemostatic proteins was carried out by comparing fragments of 12 amino acids in length, taking as related those that showed identity at ≥8 positions. <b>Results</b>. Comparative analysis of the repertoire of cellular proteins of the hemostatic system and fragments mimicking these proteins in the structure of proteins of viruses A/H1N1 1918, A(H1N1)pdm09 isolated in 2016, SARS-CoV and SARS-CoV-2, showed a significant difference between SARS-CoV-2 and analyzed viruses. In the protein structure of the SARS-CoV-2 virus, mimicry was revealed for almost all analyzed hemostasis proteins. As for the comparison of viruses A/H1N1 1918, A(H1N1)pdm09 2016 and SARS-CoV, the influenza virus A/H1N1 1918 and SARS-CoV are the closest in the repertoire of hemostatic proteins. <b>Conclusion</b>. Obtained bioinformatic analysis data can serve as a basis for further study of the role of homologous fragments in the regulation of hemostasis of the host organism.</p>","PeriodicalId":0,"journal":{"name":"","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10026243/pdf/","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.3103/S0891416822040103","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
Objective: To compare the repertoire of proteins of the human hemostatic system and fragments mimicking these proteins in the proteins of influenza A/H1N1 viruses and coronaviruses. Material and methods. Influenza viruses A/H1N1 (A/Brevig Mission/1/18), A/St. Petersburg /RII04/2016 (H1N1)pdm09, coronaviruses SARS-CoV and SARS-CoV-2 (strain Wuhan-Hu-1) were used for comparative computer analysis. The sources of the primary structures of proteins of the analyzed viruses and 41 proteins of the human hemostatic system were publicly available Internet databases, respectively, www.ncbi.nlm.nih.gov and www.nextprot.org. The search for homologous sequences in the structure of viral proteins and hemostatic proteins was carried out by comparing fragments of 12 amino acids in length, taking as related those that showed identity at ≥8 positions. Results. Comparative analysis of the repertoire of cellular proteins of the hemostatic system and fragments mimicking these proteins in the structure of proteins of viruses A/H1N1 1918, A(H1N1)pdm09 isolated in 2016, SARS-CoV and SARS-CoV-2, showed a significant difference between SARS-CoV-2 and analyzed viruses. In the protein structure of the SARS-CoV-2 virus, mimicry was revealed for almost all analyzed hemostasis proteins. As for the comparison of viruses A/H1N1 1918, A(H1N1)pdm09 2016 and SARS-CoV, the influenza virus A/H1N1 1918 and SARS-CoV are the closest in the repertoire of hemostatic proteins. Conclusion. Obtained bioinformatic analysis data can serve as a basis for further study of the role of homologous fragments in the regulation of hemostasis of the host organism.