TY - JOUR
T1 - Human astroviruses
T2 - in silico analysis of the untranslated region and putative binding sites of cellular proteins
AU - De Nova-Ocampo, Mónica
AU - Soliman, Mayra Cristina
AU - Espinosa-Hernández, Wendy
AU - Velez-del Valle, Cristina
AU - Salas-Benito, Juan
AU - Valdés-Flores, Jesús
AU - García-Morales, Lorena
N1 - Publisher Copyright:
© 2018, Springer Nature B.V.
PY - 2019/2/1
Y1 - 2019/2/1
N2 - 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.
AB - 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.
KW - RNA virus
KW - Replication
KW - SR proteins
KW - Stem-loop RNA structures
UR - http://www.scopus.com/inward/record.url?scp=85056698666&partnerID=8YFLogxK
U2 - 10.1007/s11033-018-4498-8
DO - 10.1007/s11033-018-4498-8
M3 - Artículo de revisión
C2 - 30448895
AN - SCOPUS:85056698666
SN - 0301-4851
VL - 46
SP - 1413
EP - 1424
JO - Molecular Biology Reports
JF - Molecular Biology Reports
IS - 1
ER -