PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes

• DOI: 10.1099/vir.0.19487-0
• Publication Date: 2003-11-26T23:59:02Z
• Authors: Idoia Burgui; Tomás Aragón; Juan Ortín; Amelia Nieto
• Keywords: Poly(N-isopropylacrylamide); Viral structural protein; Eukaryotic translation; Initiation factor; Viral protein

It has previously been shown that influenza virus NS1 protein enhances the translation of viral but not cellular mRNAs. This enhancement occurs by increasing rate initiation and requires 5'UTR sequence, common to all In agreement with these findings, we show here mRNAs, are associated during infection. We have reported interacts factor eIF4GI, next its poly(A)-binding 1 (PABP1)-interacting domain eIF4GI in virus-infected cells. Here NS1, although capable binding poly(A), does compete PABP1 for association and, furthermore, interact both vivo vitro an RNA-independent manner. The interaction maps between residues 365 535 81 NS1. These mapping studies, together those NS1-eIF4GI PABP1-eIF4GI interactions, imply three proteins would be compatible. Collectively, published data suggest interactions PABP1, as well could promote specific recruitment 43S complexes