title: Pyrimidine tract binding protein and La autoantigen interact differently with the 5' untranslated regions of lentiviruses and oncoretrovirus mRNAs.
abstract: Retrovirus genomic mRNA exhibits a several hundred nucleotides-long untranslated region (5' UTR) which encloses many control elements required for retrovirus replication. In addition, this 5' UTR contains translation regulatory elements, such as internal ribosome entry sites (IRESes) that have been described in oncoretroviruses, as well as in lentiviruses. UV cross-linking experiments suggested that the pyrimidine tract binding protein (PTB), a cellular protein known to regulate the activity of several picornaviral IRESes, binds to human T-cell leukemia virus (HTLV)-I RNA but not to lentiviral human immunodeficiency virus (HIV)-1, HIV-2 or simian immunodeficiency virus RNAs. To calculate the affinity of such RNA-protein interactions, we developed a new method based on the BIAcore technology. The absence of affinity of PTB for lentiviral RNAs was confirmed, whereas its affinity for HTLV-I RNAs was 1000-fold lower than for picornaviral RNAs. The BIAcore technology also revealed a significant affinity of the La autoantigen, previously described for its involvement in translational control of viral mRNAs, for HIV-1 and HTLV-I RNAs. Addition of recombinant PTB to in vitro translation experiments weakly enhanced translation initiation in the presence of HTLV-I IRES, suggesting that such an IRES requires additional trans-acting factors.
authors.affiliation: INSERM U397, Endocrinologie et Communication Cellulaire, C.H.U. Rangueil, Avenue Jean Poulhès, 31403 Toulouse Cedex 04, France.
authors.forename: A
authors.initials: A
authors.lastname: Waysbort
authors.forename: S
authors.initials: S
authors.lastname: Bonnal
authors.forename: S
authors.initials: S
authors.lastname: Audigier
authors.forename: J P
authors.initials: JP
authors.lastname: Estève
authors.forename: A C
authors.initials: AC
authors.lastname: Prats
mesh_terms: D020121:5' Untranslated Regions; D000818:Animals; D001324:Autoantigens / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015374:Biosensing Techniques; D019556:COS Cells; D004926:Escherichia coli / Q000378:metabolism; D005982:Glutathione Transferase; D015497:HIV-1 / Q000378:metabolism; D015498:HIV-2 / Q000378:metabolism; D006367:HeLa Cells; D015368:Human T-lymphotropic virus 1 / Q000378:metabolism; D006801:Humans; D019169:Jurkat Cells; D016086:Lentivirus / Q000378:metabolism*; D010957:Plasmids / Q000378:metabolism; D038941:Polypyrimidine Tract-Binding Protein; D011485:Protein Binding; D014176:Protein Biosynthesis; D012313:RNA / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000378:metabolism; D012190:Retroviridae / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015302:Simian Immunodeficiency Virus / Q000378:metabolism; D013997:Time Factors; D015533:Transcriptional Activation; D014162:Transfection; D014466:Ultraviolet Rays; D000097585:SS-B Antigen
chemical_list: D020121:5' Untranslated Regions; D001324:Autoantigens; D005982:Glutathione Transferase; D038941:Polypyrimidine Tract-Binding Protein; D012313:RNA; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D012261:Ribonucleoproteins; D000097585:SS-B Antigen