Cargando…
Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins
Human astrovirus (HAstV) constitutes a major cause of acute gastroenteritis in children. The viral 5′ and 3′ untranslated regions (UTR) have been involved in the regulation of several molecular mechanisms. However, in astrovirues have been less characterized. Here, we analyzed the secondary structur...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7089336/ https://www.ncbi.nlm.nih.gov/pubmed/30448895 http://dx.doi.org/10.1007/s11033-018-4498-8 |
_version_ | 1783509715031949312 |
---|---|
author | De Nova-Ocampo, Mónica Soliman, Mayra Cristina Espinosa-Hernández, Wendy Velez-del Valle, Cristina Salas-Benito, Juan Valdés-Flores, Jesús García-Morales, Lorena |
author_facet | De Nova-Ocampo, Mónica Soliman, Mayra Cristina Espinosa-Hernández, Wendy Velez-del Valle, Cristina Salas-Benito, Juan Valdés-Flores, Jesús García-Morales, Lorena |
author_sort | De Nova-Ocampo, Mónica |
collection | PubMed |
description | Human astrovirus (HAstV) constitutes a major cause of acute gastroenteritis in children. The viral 5′ and 3′ untranslated regions (UTR) have been involved in the regulation of several molecular mechanisms. However, in astrovirues have been less characterized. Here, we analyzed the secondary structures of the 5′ and 3′ UTR of HAstV, as well as their putative target sites that might be recognized by cellular factors. To our knowledge, this is the first bioinformatic analysis that predicts the HAstV 5′ UTR secondary structure. The analysis showed that both the UTR sequence and secondary structure are highly conserved in all HAstVs analyzed, suggesting their regulatory role of viral activities. Notably, the UTRs of HAstVs contain putative binding sites for the serine/arginine-rich factors SRSF2, SRSF5, SRSF6, SRSF3, and the multifunctional hnRNPE2 protein. More importantly, putative binding sites for PTB were localized in single-stranded RNA sequences, while hnRNPE2 sites were localized in double-stranded sequence of the HAstV 5′ and 3′ UTR structures. These analyses suggest that the combination of SRSF proteins, hnRNPE2 and PTB described here could be involved in the maintenance of the secondary structure of the HAstVs, possibly allowing the recruitment of the replication complex that selects and recruits viral RNA replication templates. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s11033-018-4498-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-7089336 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-70893362020-03-23 Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins De Nova-Ocampo, Mónica Soliman, Mayra Cristina Espinosa-Hernández, Wendy Velez-del Valle, Cristina Salas-Benito, Juan Valdés-Flores, Jesús García-Morales, Lorena Mol Biol Rep Review Human astrovirus (HAstV) constitutes a major cause of acute gastroenteritis in children. The viral 5′ and 3′ untranslated regions (UTR) have been involved in the regulation of several molecular mechanisms. However, in astrovirues have been less characterized. Here, we analyzed the secondary structures of the 5′ and 3′ UTR of HAstV, as well as their putative target sites that might be recognized by cellular factors. To our knowledge, this is the first bioinformatic analysis that predicts the HAstV 5′ UTR secondary structure. The analysis showed that both the UTR sequence and secondary structure are highly conserved in all HAstVs analyzed, suggesting their regulatory role of viral activities. Notably, the UTRs of HAstVs contain putative binding sites for the serine/arginine-rich factors SRSF2, SRSF5, SRSF6, SRSF3, and the multifunctional hnRNPE2 protein. More importantly, putative binding sites for PTB were localized in single-stranded RNA sequences, while hnRNPE2 sites were localized in double-stranded sequence of the HAstV 5′ and 3′ UTR structures. These analyses suggest that the combination of SRSF proteins, hnRNPE2 and PTB described here could be involved in the maintenance of the secondary structure of the HAstVs, possibly allowing the recruitment of the replication complex that selects and recruits viral RNA replication templates. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s11033-018-4498-8) contains supplementary material, which is available to authorized users. Springer Netherlands 2018-11-17 2019 /pmc/articles/PMC7089336/ /pubmed/30448895 http://dx.doi.org/10.1007/s11033-018-4498-8 Text en © Springer Nature B.V. 2018 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Review De Nova-Ocampo, Mónica Soliman, Mayra Cristina Espinosa-Hernández, Wendy Velez-del Valle, Cristina Salas-Benito, Juan Valdés-Flores, Jesús García-Morales, Lorena Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins |
title | Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins |
title_full | Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins |
title_fullStr | Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins |
title_full_unstemmed | Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins |
title_short | Human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins |
title_sort | human astroviruses: in silico analysis of the untranslated region and putative binding sites of cellular proteins |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7089336/ https://www.ncbi.nlm.nih.gov/pubmed/30448895 http://dx.doi.org/10.1007/s11033-018-4498-8 |
work_keys_str_mv | AT denovaocampomonica humanastrovirusesinsilicoanalysisoftheuntranslatedregionandputativebindingsitesofcellularproteins AT solimanmayracristina humanastrovirusesinsilicoanalysisoftheuntranslatedregionandputativebindingsitesofcellularproteins AT espinosahernandezwendy humanastrovirusesinsilicoanalysisoftheuntranslatedregionandputativebindingsitesofcellularproteins AT velezdelvallecristina humanastrovirusesinsilicoanalysisoftheuntranslatedregionandputativebindingsitesofcellularproteins AT salasbenitojuan humanastrovirusesinsilicoanalysisoftheuntranslatedregionandputativebindingsitesofcellularproteins AT valdesfloresjesus humanastrovirusesinsilicoanalysisoftheuntranslatedregionandputativebindingsitesofcellularproteins AT garciamoraleslorena humanastrovirusesinsilicoanalysisoftheuntranslatedregionandputativebindingsitesofcellularproteins |