Poly(A)-binding protein binds to the non-polyadenylated 3′ untranslated region of dengue virus and modulates translation efficiency

2009/02/13 by Charlotta Polacek, Peter Friebe, Eva Harris · 1 voice
Agricultural and Biological Sciences · Medicine · #Mosquito-borne diseases and control #Vector-Borne Animal Diseases #Viral Infections and Immunology Research

paper · doi:10.1099/vir.0.007021-0

openalex publication_date 2009/02/13 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/15

Abstract

Poly(A)-binding protein (PABP) is a key player in mRNA circularization and translation initiation of polyadenylated mRNAs. It simultaneously binds the 3' poly(A) tail of an mRNA and eukaryotic initiation factor 4G (eIF4G), which forms part of the translation initiation complex assembling at the 5'end, thus circularizing the RNA molecule and enhancing translation initiation. Here, we report the binding of PABP to the non-polyadenylated 3'end of dengue virus (DENV) RNA. PABP binds the DENV 3' untranslated region (3'UTR) internally, upstream of the conserved 3'stem-loop near the two dumb-bell structures, and can be displaced by poly(A) RNA. The PABP-specific translation inhibitor PABP-interacting protein 2 (Paip2) interferes with the DENV 3'UTR-PABP interaction, and in vitro translation of DENV reporter RNAs in baby hamster kidney cell extracts is inhibited by Paip2 in a dose-dependent manner. Our findings show an expanded translation mechanism for PABP, binding to a viral RNA lacking a terminal poly(A) tail.

Citations

• End-to-end communication in the modulation of translation by mammalian RNA viruses
• Rotavirus RNA‐binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F

Discussions

• Summary The mRNA of most — but not all — RNA viruses is polyadenylated. In the case of cytoplasmic-replicating positive-strand RNA viruses — where the genomic RNA also acts as mRNA — the genomic RNA i [stackexchange, 3 points]

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