La, PTB, and PAB proteins bind to the 3′ untranslated region of Norwalk virus genomic RNA

• Published in: Biochemical and biophysical research communications 2003-11, Vol.311 (3), p.759-766
• Main Authors: Gutiérrez-Escolano, Ana Lorena, Vázquez-Ochoa, Melina, Escobar-Herrera, Jaime, Hernández-Acosta, Javier
• Format: Article
• Language: English
• Subjects: 3' Untranslated Regions; 3′UTR; Autoantigens; Bacterial Proteins - chemistry; Base Sequence; Carrier Proteins - chemistry; HeLa Cells; Humans; Intracellular Signaling Peptides and Proteins; La protein; Molecular Sequence Data; Norwalk virus; Norwalk virus - genetics; Nucleic Acid Conformation; PAB protein; PABP protein; Poly A; Polypyrimidine Tract-Binding Protein - chemistry; Precipitin Tests; Protein Binding; Protein Biosynthesis; PTB protein; Recombinant Proteins - metabolism; Replication; Ribonucleoproteins - chemistry; RNA - genetics; RNA - metabolism; RNA–protein interactions; SS-B Antigen; Transcription, Genetic; Ultraviolet Rays
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2003.10.066

Noroviruses are human enteric caliciviruses for which no cell culture is available. Consequently, the mechanisms and factors involved in their replication have been difficult to study. In an attempt to analyze the cis- and trans-acting factors that could have a role in NV replication, the 3′-untranslated region of the genome was studied. Use of Zuker’s mfold-2 software predicted that NV 3′UTR contains a stem-loop structure of 47 nts. Proteins from HeLa cell extracts, such as La and PTB, form stable complexes with this region. The addition of a poly(A) tail (24 nts) to the 3′UTR permits the specific binding of the poly(A) binding protein (PABP) present in HeLa cell extracts, as well as the recombinant PABP. Since La, PTB, and PABP are important trans-acting factors required for viral translation and replication, these RNA–protein interactions may play a role in NV replication or translation.