In silico analysis of the aggregation propensity of the SARS-CoV-2 proteome: Insight into possible cellular pathologies
| العنوان: | In silico analysis of the aggregation propensity of the SARS-CoV-2 proteome: Insight into possible cellular pathologies |
|---|---|
| المؤلفون: | Anita Krisko, Tiago F. Outeiro, Manuel Flores-León, Diana F. Lázaro, Liana Shvachiy |
| المصدر: | Biochimica et biophysica acta / Proteins and proteomics 1869(10), 140693 (2021). doi:10.1016/j.bbapap.2021.140693 Biochimica et Biophysica Acta. Proteins and Proteomics |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | Proteome, metabolism [Viral Proteins], Bioinformatics, In silico, viruses, Biophysics, Plasma protein binding, Disease, Protein aggregation, Biology, medicine.disease_cause, APR, aggregation-prone regions, Virus Replication, Biochemistry, pathogenicity [SARS-CoV-2], Analytical Chemistry, CoVex, Coronavirus Explorer, metabolism [SARS-CoV-2], 03 medical and health sciences, Open Reading Frames, Viral Proteins, 0302 clinical medicine, ORF, open reading frame, PDB, Protein Data Bank, ddc:570, medicine, Molecular Biology, 030304 developmental biology, Coronavirus, Genetics, 0303 health sciences, SARS-CoV-2, Severe acute respiratory syndrome coronavirus 2, PASTA, prediction of amyloid structural aggregation, SARS-CoV-2, genetics [SARS-CoV-2], Entry into host, 3. Good health, Proteostasis, Mutation, NSP, non-structural proteins, A3D, Aggrescan3D, 030217 neurology & neurosurgery, COVID-19, coronavirus disease 19, Research Paper, Protein Binding |
| الوصف: | The SARS-CoV-2 virus causes the coronavirus disease 19 emerged in 2020. The pandemic triggered a turmoil in public health and is having a tremendous social and economic impact around the globe. Upon entry into host cells, the SARS-CoV-2 virus hijacks cellular machineries to produce and maintain its own proteins, spreading the infection. Although the disease is known for prominent respiratory symptoms, accumulating evidence is also demonstrating the involvement of the central nervous system, with possible mid- and long-term neurological consequences. In this study, we conducted a detailed bioinformatic analysis of the SARS-CoV-2 proteome aggregation propensity by using several complementary computational tools. Our study identified 10 aggregation prone proteins in the reference SARS-CoV-2 strain: the non-structural proteins Nsp4, Nsp6 and Nsp7 as well as ORF3a, ORF6, ORF7a, ORF7b, ORF10, CovE and CovM. By searching for the available mutants of each protein, we have found that most proteins are conserved, while ORF3a and ORF7b are variable and characterized by the occurrence of a large number of mutants with increased aggregation propensity. The geographical distribution of the mutants revealed interesting differences in the localization of aggregation-prone mutants of each protein. Aggregation-prone mutants of ORF7b were found in 7 European countries, whereas those of ORF3a in only 2. Aggregation-prone sequences of ORF7b, but not of ORF3a, were identified in Australia, India, Nepal, China, and Thailand. Our results are important for future analysis of a possible correlation between higher transmissibility and infection, as well as the presence of neurological symptoms with aggregation propensity of SARS-CoV-2 proteins. |
| اللغة: | English |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c5e3302f41d3ee8b3a2526f7302e165Test https://pub.dzne.de/record/155650Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....7c5e3302f41d3ee8b3a2526f7302e165 |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |