This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rojas-Eisenring, I. A. Articles by del Angel, R. M. Search for Related Content PubMed PubMed Citation Articles by Rojas-Eisenring, I. A. Articles by del Angel, R. M.

 Previous Article  |  Next Article 

J. Virol., Nov 1995, 6819-6824, Vol 69, No. 11
Copyright © 1995, American Society for Microbiology

Cell proteins bind to a linear polypyrimidine-rich sequence within the 5'-untranslated region of rhinovirus 14 RNA

IA Rojas-Eisenring, M Cajero-Juarez and RM del Angel
Departamento de Patologia Experimental, Instituto Politecnico Nacional, Mexico City, Mexico.

Members of the picornavirus family initiate translation of their RNA genomes by a cap-independent mechanism in which ribosomes bind to an internal site in the 5' untranslated region (5'-UTR). This unique process requires an internal ribosome entry site (IRES), a highly structured RNA whose function is mediated in part by interactions with cell proteins. The IRES element of human rhinovirus 2 (HRV-2) extends from nucleotide (nt) 10 to between nt 544 and 568 and has been shown to interact with two cell proteins, pyrimidine tract-binding protein (pPTB) and p97. To map the specific regions of HRV-14 RNA that bind cell proteins, mobility shift, UV cross-linking and Western immunoblot analyses were performed. The results indicate that an RNA sequence from nt 538 to 591 interacts with pPTB and La, two proteins previously shown to functionally interact with the IRES elements of several picornaviruses. Two additional proteins, p97 and p68, were also cross- linked to nt 538 to 591 RNA. These four proteins interact with a putatively unstructured portion of the 5'-UTR that contains a polypyrimidine tract and has been shown to be present at the 3' border of sequences that are essential for IRES function of HRV-2. These protein-RNA interactions are likely to play a role in internal initiation of translation.

This article has been cited by other articles:

• Yocupicio-Monroy, R. M. E., Medina, F., Reyes-del Valle, J., del Angel, R. M. (2003). Cellular Proteins from Human Monocytes Bind to Dengue 4 Virus Minus-Strand 3' Untranslated Region RNA. J. Virol. 77: 3067-3076 [Abstract] [Full Text]  
• Fukushi, S., Okada, M., Stahl, J., Kageyama, T., Hoshino, F. B., Katayama, K. (2001). Ribosomal Protein S5 Interacts with the Internal Ribosomal Entry Site of Hepatitis C Virus. J. Biol. Chem. 276: 20824-20826 [Abstract] [Full Text]