{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T01:06:31Z","timestamp":1788570391186,"version":"build-2803163510"},"reference-count":75,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2024,11,9]],"date-time":"2024-11-09T00:00:00Z","timestamp":1731110400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Agencia Nacional de Investigaci\u00f3n y Desarrollo (ANID), Gobierno de Chile","award":["FONDECYT 1210736"],"award-info":[{"award-number":["FONDECYT 1210736"]}]},{"name":"Agencia Nacional de Investigaci\u00f3n y Desarrollo (ANID), Gobierno de Chile","award":["ICM ANID ICN2021_045"],"award-info":[{"award-number":["ICM ANID ICN2021_045"]}]},{"name":"Agencia Nacional de Investigaci\u00f3n y Desarrollo (ANID), Gobierno de Chile","award":["21160121"],"award-info":[{"award-number":["21160121"]}]},{"name":"Agencia Nacional de Investigaci\u00f3n y Desarrollo (ANID), Gobierno de Chile","award":["ACT1408"],"award-info":[{"award-number":["ACT1408"]}]},{"name":"Iniciativa Cientifica Milenio (ICM), Instituto Milenio de Inmunolog\u00eda e Inmunoterapia","award":["FONDECYT 1210736"],"award-info":[{"award-number":["FONDECYT 1210736"]}]},{"name":"Iniciativa Cientifica Milenio (ICM), Instituto Milenio de Inmunolog\u00eda e Inmunoterapia","award":["ICM ANID ICN2021_045"],"award-info":[{"award-number":["ICM ANID ICN2021_045"]}]},{"name":"Iniciativa Cientifica Milenio (ICM), Instituto Milenio de Inmunolog\u00eda e Inmunoterapia","award":["21160121"],"award-info":[{"award-number":["21160121"]}]},{"name":"Iniciativa Cientifica Milenio (ICM), Instituto Milenio de Inmunolog\u00eda e Inmunoterapia","award":["ACT1408"],"award-info":[{"award-number":["ACT1408"]}]},{"name":"ONICYT-Doctoral Fellowships","award":["FONDECYT 1210736"],"award-info":[{"award-number":["FONDECYT 1210736"]}]},{"name":"ONICYT-Doctoral Fellowships","award":["ICM ANID ICN2021_045"],"award-info":[{"award-number":["ICM ANID ICN2021_045"]}]},{"name":"ONICYT-Doctoral Fellowships","award":["21160121"],"award-info":[{"award-number":["21160121"]}]},{"name":"ONICYT-Doctoral Fellowships","award":["ACT1408"],"award-info":[{"award-number":["ACT1408"]}]},{"name":"Proyecto CONICYT-PIA","award":["FONDECYT 1210736"],"award-info":[{"award-number":["FONDECYT 1210736"]}]},{"name":"Proyecto CONICYT-PIA","award":["ICM ANID ICN2021_045"],"award-info":[{"award-number":["ICM ANID ICN2021_045"]}]},{"name":"Proyecto CONICYT-PIA","award":["21160121"],"award-info":[{"award-number":["21160121"]}]},{"name":"Proyecto CONICYT-PIA","award":["ACT1408"],"award-info":[{"award-number":["ACT1408"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>Dengue virus (DENV) is an enveloped, positive sense, single-stranded RNA virus belonging to the Flaviviridae. Translation initiation of the DENV mRNA (vRNA) can occur following a cap-dependent, 5\u2032-3\u2019end-dependent internal ribosome entry site (IRES)-independent or IRES-dependent mechanism. This study evaluated the activity of DENV IRES in BHK-21 cells and the role of the polypyrimidine-tract binding protein (PTB) isoforms PTB1, PTB2, and PTB4 as IRES-transacting factors (ITAFs) for the DENV IRES. The results show that DENV-IRES activity is stimulated in DENV-replicating BHK-21 cells and cells expressing the Foot-and-mouth\u00a0disease virus leader or Human rhinovirus 2A proteases. Protease activity was necessary, although a complete shutdown of cap-dependent translation initiation was not a requirement to stimulate DENV IRES activity. Regarding PTB, the results show that PTB1 &gt; PTB2 &gt; PTB4 stimulates DENV-IRES activity in BHK-21 cells. Mutations in the PTB RNA recognition motifs (RRMs), RRM1\/RRM2 or RRM3\/RRM4, differentially impact PTB1, PTB2, and PTB4\u2019s ability to promote DENV IRES-mediated translation initiation in BHK-21 cells. PTB1-induced DENV-IRES stimulation is rescinded when RRM1\/RRM2 or RRM3\/RRM4 are disrupted. Mutations in RRM1\/RRM2 or RRM3\/RRM4 do not affect the ITAF activity of PTB2. Mutating RRM3\/RRM4, but not RRM1\/RRM2, abolishes the ability of PTB4 to stimulate the DENV IRES. Thus, PTB1, PTB2, and PTB4 are ITAFs for the DENV IRES.<\/jats:p>","DOI":"10.3390\/v16111757","type":"journal-article","created":{"date-parts":[[2024,11,11]],"date-time":"2024-11-11T03:52:07Z","timestamp":1731297127000},"page":"1757","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["The Polypyrimidine Tract-Binding Protein Is a Transacting Factor for the Dengue Virus Internal Ribosome Entry Site"],"prefix":"10.3390","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5981-5632","authenticated-orcid":false,"given":"Leandro","family":"Fern\u00e1ndez-Garc\u00eda","sequence":"first","affiliation":[{"name":"Laboratorio de Virolog\u00eda Molecular, Instituto Milenio de Inmunolog\u00eda e Inmunoterapia, Departamento de Enfermedades Infecciosas e Inmunolog\u00eda Pedi\u00e1trica, Centro de Investigaciones M\u00e9dicas, Escuela de Medicina, Pontificia Universidad Cat\u00f3lica de Chile, Marcoleta 391, Santiago 8330024, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0471-4751","authenticated-orcid":false,"given":"Jenniffer","family":"Angulo","sequence":"additional","affiliation":[{"name":"Laboratorio de Virolog\u00eda Molecular, Instituto Milenio de Inmunolog\u00eda e Inmunoterapia, Departamento de Enfermedades Infecciosas e Inmunolog\u00eda Pedi\u00e1trica, Centro de Investigaciones M\u00e9dicas, Escuela de Medicina, Pontificia Universidad Cat\u00f3lica de Chile, Marcoleta 391, Santiago 8330024, Chile"},{"name":"Facultad de Ciencias Biol\u00f3gicas, Pontificia Universidad Cat\u00f3lica de Chile, Avenida Libertador Bernardo O\u2019Higgins 340, Santiago 8331150, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7936-8478","authenticated-orcid":false,"given":"Marcelo","family":"L\u00f3pez-Lastra","sequence":"additional","affiliation":[{"name":"Laboratorio de Virolog\u00eda Molecular, Instituto Milenio de Inmunolog\u00eda e Inmunoterapia, Departamento de Enfermedades Infecciosas e Inmunolog\u00eda Pedi\u00e1trica, Centro de Investigaciones M\u00e9dicas, Escuela de Medicina, Pontificia Universidad Cat\u00f3lica de Chile, Marcoleta 391, Santiago 8330024, Chile"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,11,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nature12060","article-title":"The global distribution and burden of dengue","volume":"496","author":"Bhatt","year":"2013","journal-title":"Nature"},{"key":"ref_2","first-page":"15","article-title":"Control of dengue virus translation and replication","volume":"338","author":"Paranjape","year":"2010","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"4448","DOI":"10.1021\/acs.chemrev.7b00719","article-title":"Biochemistry and Molecular Biology of Flaviviruses","volume":"118","author":"Barrows","year":"2018","journal-title":"Chem. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.virol.2004.08.004","article-title":"Enhancement of dengue virus translation: Role of the 3\u2032 untranslated region and the terminal 3\u2032 stem-loop domain","volume":"329","author":"Holden","year":"2004","journal-title":"Virology"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"2976","DOI":"10.1128\/JVI.80.6.2976-2986.2006","article-title":"Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited","volume":"80","author":"Edgil","year":"2006","journal-title":"J. Virol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"e00459-19","DOI":"10.1128\/mBio.00459-19","article-title":"Dengue and Zika Virus 5\u2032 Untranslated Regions Harbor Internal Ribosomal Entry Site Functions","volume":"10","author":"Song","year":"2019","journal-title":"MBio"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"e01998-20","DOI":"10.1128\/JVI.01998-20","article-title":"The internal ribosome entry site of the Dengue virus mRNA is active when cap-dependent translation initiation is inhibited","volume":"95","author":"Angulo","year":"2021","journal-title":"J. Virol."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Merrick, W.C., and Pavitt, G.D. (2018). Protein Synthesis Initiation in Eukaryotic Cells. Cold Spring Harb. Perspect. Biol., 10.","DOI":"10.1101\/cshperspect.a033092"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1146\/annurev-biochem-013118-111042","article-title":"The Organizing Principles of Eukaryotic Ribosome Recruitment","volume":"88","author":"Pelletier","year":"2019","journal-title":"Annu. Rev. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Mailliot, J., and Martin, F. (2018). Viral internal ribosomal entry sites: Four classes for one goal. Wiley Interdiscip. Rev. RNA, 9.","DOI":"10.1002\/wrna.1458"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Kwan, T., and Thompson, S.R. (2019). Noncanonical Translation Initiation in Eukaryotes. Cold Spring Harb. Perspect. Biol., 11.","DOI":"10.1101\/cshperspect.a032672"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Lopez-Ulloa, B., Fuentes, Y., Pizarro-Ortega, M.S., and Lopez-Lastra, M. (2022). RNA-Binding Proteins as Regulators of Internal Initiation of Viral mRNA Translation. Viruses, 14.","DOI":"10.3390\/v14020188"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1128\/iai.11.2.330-333.1975","article-title":"Influence of cell type and virus upon virus-specific immune cytolysis","volume":"11","author":"Brandt","year":"1975","journal-title":"Infect. Immun."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Shrivastava, N., Sripada, S., Kaur, J., Shah, P.S., and Cecilia, D. (2011). Insights into the internalization and retrograde trafficking of Dengue 2 virus in BHK-21 cells. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025229"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"6631","DOI":"10.1128\/JVI.79.11.6631-6643.2005","article-title":"Long-range RNA-RNA interactions circularize the dengue virus genome","volume":"79","author":"Alvarez","year":"2005","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"4990","DOI":"10.1128\/MCB.20.14.4990-4999.2000","article-title":"Naturally occurring dicistronic cricket paralysis virus RNA is regulated by two internal ribosome entry sites","volume":"20","author":"Wilson","year":"2000","journal-title":"Mol. Cell Biol."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Angulo, J., Caceres, C.J., Contreras, N., Fernandez-Garcia, L., Chamond, N., Ameur, M., Sargueil, B., and Lopez-Lastra, M. (2022). Polypyrimidine-Tract-Binding Protein Isoforms Differentially Regulate the Hepatitis C Virus Internal Ribosome Entry Site. Viruses, 15.","DOI":"10.3390\/v15010008"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1093\/nar\/gkn1022","article-title":"Analysis of natural variants of the hepatitis C virus internal ribosome entry site reveals that primary sequence plays a key role in cap-independent translation","volume":"37","author":"Barria","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"11030","DOI":"10.1093\/nar\/gky802","article-title":"Non-canonical translation initiation of the spliced mRNA encoding the human T-cell leukemia virus type 1 basic leucine zipper protein","volume":"46","author":"Caceres","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"E877","DOI":"10.1210\/jc.2013-1126","article-title":"The relationship between vitamin D status and adrenal insufficiency in critically ill children","volume":"98","author":"McNally","year":"2013","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"5215","DOI":"10.1093\/nar\/gkr086","article-title":"Activation of a microRNA response in trans reveals a new role for poly(A) in translational repression","volume":"39","author":"Ricci","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"3745","DOI":"10.1038\/emboj.2012.220","article-title":"DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs","volume":"31","author":"Rubilar","year":"2012","journal-title":"EMBO J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1006\/viro.1993.1267","article-title":"The two species of the foot-and-mouth disease virus leader protein, expressed individually, exhibit the same activities","volume":"194","author":"Medina","year":"1993","journal-title":"Virology"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"427","DOI":"10.4269\/ajtmh.2001.65.427","article-title":"Replication of dengue virus type 2 in human monocyte-derived macrophages: Comparisons of isolates and recombinant viruses with substitutions at amino acid 390 in the envelope glycoprotein","volume":"65","author":"Pryor","year":"2001","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1880","DOI":"10.1111\/febs.13708","article-title":"Polypyrimidine tract-binding protein binds to the 5\u2032 untranslated region of the mouse mammary tumor virus mRNA and stimulates cap-independent translation initiation","volume":"283","author":"Caceres","year":"2016","journal-title":"FEBS J."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"4765","DOI":"10.1093\/nar\/gkt168","article-title":"MBNL1 and PTB cooperate to repress splicing of Tpm1 exon 3","volume":"41","author":"Gooding","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1093\/nar\/gkv1325","article-title":"LOOP IIId of the HCV IRES is essential for the structural rearrangement of the 40S-HCV IRES complex","volume":"44","author":"Angulo","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Vallejos, M., Carvajal, F., Pino, K., Navarrete, C., Ferres, M., Huidobro-Toro, J.P., Sargueil, B., and Lopez-Lastra, M. (2012). Functional and structural analysis of the internal ribosome entry site present in the mRNA of natural variants of the HIV-1. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0035031"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.antiviral.2016.09.006","article-title":"Targeting deoxyhypusine hydroxylase activity impairs cap-independent translation initiation driven by the 5\u2032untranslated region of the HIV-1, HTLV-1, and MMTV mRNAs","volume":"134","author":"Caceres","year":"2016","journal-title":"Antiviral Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Yuan, J.S., Reed, A., Chen, F., and Stewart, C.N. (2006). Statistical analysis of real-time PCR data. BMC Bioinform., 7.","DOI":"10.1186\/1471-2105-7-85"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"10479","DOI":"10.1093\/nar\/gkaa765","article-title":"Post-translational modifications of hnRNP A1 differentially modulate retroviral IRES-mediated translation initiation","volume":"48","author":"Barrera","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/nmeth.1314","article-title":"SUnSET, a nonradioactive method to monitor protein synthesis","volume":"6","author":"Schmidt","year":"2009","journal-title":"Nat. Methods"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/s13007-016-0120-z","article-title":"Use of the non-radioactive SUnSET method to detect decreased protein synthesis in proteasome inhibited Arabidopsis roots","volume":"12","year":"2016","journal-title":"Plant Methods"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"21975","DOI":"10.1074\/jbc.270.37.21975","article-title":"Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. Implications for cap-dependent and cap-independent translational initiation","volume":"270","author":"Lamphear","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3271","DOI":"10.1128\/JVI.78.7.3271-3278.2004","article-title":"Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: Identification of the L-protease cleavage site in vitro","volume":"78","author":"Gradi","year":"2004","journal-title":"J. Virol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1002\/j.1460-2075.1996.tb00479.x","article-title":"The C-terminal domain of eukaryotic protein synthesis initiation factor (eIF) 4G is sufficient to support cap-independent translation in the absence of eIF4E","volume":"15","author":"Ohlmann","year":"1996","journal-title":"Embo J."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"e02150-16","DOI":"10.1128\/mBio.02150-16","article-title":"Flavivirus Infection Uncouples Translation Suppression from Cellular Stress Responses","volume":"8","author":"Roth","year":"2017","journal-title":"mBio"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1093\/nar\/25.5.925","article-title":"Comparison of picornaviral IRES-driven internal initiation of translation in cultured cells of different origins","volume":"25","author":"Borman","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/S0014-5793(00)01928-1","article-title":"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro","volume":"480","author":"Glaser","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3467","DOI":"10.1128\/JVI.73.4.3467-3472.1999","article-title":"Eukaryotic initiation factor 4GII (eIF4GII), but not eIF4GI, cleavage correlates with inhibition of host cell protein synthesis after human rhinovirus infection","volume":"73","author":"Svitkin","year":"1999","journal-title":"J. Virol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"8444","DOI":"10.1128\/jvi.70.12.8444-8450.1996","article-title":"The eIF4G-eIF4E complex is the target for direct cleavage by the rhinovirus 2A proteinase","volume":"70","author":"Haghighat","year":"1996","journal-title":"J. Virol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"4942","DOI":"10.1093\/nar\/gks172","article-title":"Gemin5 proteolysis reveals a novel motif to identify L protease targets","volume":"40","author":"Pineiro","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"e02472-16","DOI":"10.1128\/JVI.02472-16","article-title":"Differential Disruption of Nucleocytoplasmic Trafficking Pathways by Rhinovirus 2A Proteases","volume":"91","author":"Watters","year":"2017","journal-title":"J. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"10874","DOI":"10.1128\/JVI.00718-11","article-title":"Differential processing of nuclear pore complex proteins by rhinovirus 2A proteases from different species and serotypes","volume":"85","author":"Watters","year":"2011","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S0168-1702(99)00039-8","article-title":"Rhinovirus 2A proteinase mediated stimulation of rhinovirus RNA translation is additive to the stimulation effected by cellular RNA binding proteins","volume":"62","author":"Hunt","year":"1999","journal-title":"Virus Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3465","DOI":"10.1128\/jvi.69.6.3465-3474.1995","article-title":"Foot-and-mouth disease virus Lb proteinase can stimulate rhinovirus and enterovirus IRES-driven translation and cleave several proteins of cellular and viral origin","volume":"69","author":"Ziegler","year":"1995","journal-title":"J. Virol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/S0042-6822(95)90001-2","article-title":"Picornavirus 2A proteinase-mediated stimulation of internal initiation of translation is dependent on enzymatic activity and the cleavage products of cellular proteins","volume":"213","author":"Ziegler","year":"1995","journal-title":"Virology"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.tim.2017.01.010","article-title":"Regulation Mechanisms of Viral IRES-Driven Translation","volume":"25","author":"Lee","year":"2017","journal-title":"Trends Microbiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1042\/BST0360641","article-title":"Polypyrimidine-tract-binding protein: A multifunctional RNA-binding protein","volume":"36","author":"Sawicka","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Castillo, J.A., Castrillon, J.C., Diosa-Toro, M., Betancur, J.G., St Laurent, G., Smit, J.M., and Urcuqui-Inchima, S. (2016). Complex interaction between dengue virus replication and expression of miRNA-133a. BMC Infect. Dis., 16.","DOI":"10.1186\/s12879-016-1364-y"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2893","DOI":"10.1099\/vir.0.013433-0","article-title":"Polypyrimidine tract-binding protein is relocated to the cytoplasm and is required during dengue virus infection in Vero cells","volume":"90","author":"Galvan","year":"2009","journal-title":"J. Gen. Virol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.bbrc.2009.05.036","article-title":"Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus","volume":"385","author":"Jiang","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"17021","DOI":"10.1074\/jbc.M109.006239","article-title":"The polypyrimidine tract-binding protein is required for efficient dengue virus propagation and associates with the viral replication machinery","volume":"284","author":"Anwar","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Viktorovskaya, O.V., Greco, T.M., Cristea, I.M., and Thompson, S.R. (2016). Identification of RNA Binding Proteins Associated with Dengue Virus RNA in Infected Cells Reveals Temporally Distinct Host Factor Requirements. PLoS Negl. Trop. Dis., 10.","DOI":"10.1371\/journal.pntd.0004921"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1017\/S1355838299981414","article-title":"Polypyrimidine-tract binding protein (PTB) is necessary, but not sufficient, for efficient internal initiation of translation of human rhinovirus-2 RNA","volume":"5","author":"Hunt","year":"1999","journal-title":"RNA"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Hamiti, M., Zhang, X.T., Zhu, R.M., Liu, Y.P., Yin, B., Shu, P.C., and Peng, X.Z. (2024). Polypyrimidine Tract-Binding Protein Enhances Zika Virus Translation by Binding to the 5\u2032 UTR of Internal Ribosomal Entry Site. Chin. Med. Sci. J.","DOI":"10.24920\/004393"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"5881","DOI":"10.1093\/nar\/gkp623","article-title":"The human insulin receptor mRNA contains a functional internal ribosome entry segment","volume":"37","author":"Spriggs","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1017\/S1355838201010214","article-title":"Differential alternative splicing activity of isoforms of polypyrimidine tract binding protein (PTB)","volume":"7","author":"Wollerton","year":"2001","journal-title":"RNA"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1006\/viro.2002.1407","article-title":"Translation elongation factor-1alpha, La, and PTB interact with the 3\u2032 untranslated region of dengue 4 virus RNA","volume":"295","year":"2002","journal-title":"Virology"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"2054","DOI":"10.1126\/science.1114066","article-title":"Structure of PTB bound to RNA: Specific binding and implications for splicing regulation","volume":"309","author":"Oberstrass","year":"2005","journal-title":"Science"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1261\/rna.2549411","article-title":"Activation of picornaviral IRESs by PTB shows differential dependence on each PTB RNA-binding domain","volume":"17","author":"Kafasla","year":"2011","journal-title":"RNA"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1038\/sj.emboj.7600911","article-title":"Structure of the two most C-terminal RNA recognition motifs of PTB using segmental isotope labeling","volume":"25","author":"Vitali","year":"2006","journal-title":"EMBO J."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Hou, J.N., Chen, T.H., Chiang, Y.H., Peng, J.Y., Yang, T.H., Cheng, C.C., Sofiyatun, E., Chiu, C.H., Chiang-Ni, C., and Chen, W.J. (2017). PERK Signal-Modulated Protein Translation Promotes the Survivability of Dengue 2 Virus-Infected Mosquito Cells and Extends Viral Replication. Viruses, 9.","DOI":"10.3390\/v9090262"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1126\/science.aad9868","article-title":"Translational control by 5\u2032-untranslated regions of eukaryotic mRNAs","volume":"352","author":"Hinnebusch","year":"2016","journal-title":"Science"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.gene.2004.02.051","article-title":"Cap-dependent and cap-independent translation in eukaryotic systems","volume":"332","author":"Merrick","year":"2004","journal-title":"Gene"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1017\/S1355838200001679","article-title":"Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system","volume":"6","author":"Bergamini","year":"2000","journal-title":"RNA"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1093\/nar\/gkn979","article-title":"A novel role for Gemin5 in mRNA translation","volume":"37","author":"Pacheco","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1093\/nar\/gks1212","article-title":"Gemin5 promotes IRES interaction and translation control through its C-terminal region","volume":"41","author":"Pineiro","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"28796","DOI":"10.1074\/jbc.M110.143404","article-title":"Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease","volume":"285","author":"Park","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1631","DOI":"10.1016\/j.str.2004.07.008","article-title":"Structure and RNA interactions of the N-terminal RRM domains of PTB","volume":"12","author":"Simpson","year":"2004","journal-title":"Structure"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"3132","DOI":"10.1093\/emboj\/19.12.3132","article-title":"Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold","volume":"19","author":"Conte","year":"2000","journal-title":"EMBO J."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"4105","DOI":"10.1073\/pnas.0907072107","article-title":"RNA looping by PTB: Evidence using FRET and NMR spectroscopy for a role in splicing repression","volume":"107","author":"Lamichhane","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"5026","DOI":"10.1128\/JVI.77.8.5026-5029.2003","article-title":"Human rhinovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different","volume":"77","author":"Gradi","year":"2003","journal-title":"J. Virol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"19200","DOI":"10.1016\/S0021-9258(19)36499-3","article-title":"Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus","volume":"268","author":"Lamphear","year":"1993","journal-title":"J. Biol. Chem."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/16\/11\/1757\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:29:30Z","timestamp":1760113770000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/16\/11\/1757"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11,9]]},"references-count":75,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2024,11]]}},"alternative-id":["v16111757"],"URL":"https:\/\/doi.org\/10.3390\/v16111757","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,11,9]]}}}