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This review analyzes the structural characteristics of eEF1A and the eEF1B complex, and their regulatory mechanisms during viral infection. eEF1A impacts viral replication by stabilizing viral RNA-dependent RNA polymerase (RdRp) complexes, modulating genomic RNA synthesis, and facilitating viral assembly through cytoskeletal regulation. eEF1B subunits contribute through enhancing viral mRNA translation, regulating nuclear transport of viral components, and mediating post-translational modifications. The high conservation of eEF1 proteins across species and their involvement in multiple stages of viral replication establish them as promising broad-spectrum antiviral targets. Current eEF1-targeting compounds like plitidepsin demonstrate efficacy against diverse viral families, though therapeutic development faces challenges in balancing antiviral activity with host toxicity. This review provides a theoretical foundation for developing novel antiviral strategies targeting host\u2013virus interaction interfaces and offers insights into addressing emerging infectious diseases.<\/jats:p>","DOI":"10.3390\/v17050682","type":"journal-article","created":{"date-parts":[[2025,5,7]],"date-time":"2025-05-07T08:20:53Z","timestamp":1746606053000},"page":"682","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Multidimensional Regulatory Mechanisms and Targeting Strategies of the eEF1 Family in RNA Virus Infection"],"prefix":"10.3390","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-4273-5653","authenticated-orcid":false,"given":"Xin","family":"Wang","sequence":"first","affiliation":[{"name":"Key Laboratory of Avian Bioproducts Development, College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2685-6520","authenticated-orcid":false,"given":"Kaituo","family":"Liu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Avian Bioproducts Development, College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonosis, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Key Laboratory of Zoonosis, Yangzhou University, Yangzhou 225009, China"},{"name":"Joint International Research Laboratory of Agriculture and Agri-Product Safety, The Ministry of Education of China, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9699-2766","authenticated-orcid":false,"given":"Xiaoquan","family":"Wang","sequence":"additional","affiliation":[{"name":"Key Laboratory of Avian Bioproducts Development, College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonosis, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Key Laboratory of Zoonosis, Yangzhou University, Yangzhou 225009, China"},{"name":"Joint International Research Laboratory of Agriculture and Agri-Product Safety, The Ministry of Education of China, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9924-6646","authenticated-orcid":false,"given":"Xiufan","family":"Liu","sequence":"additional","affiliation":[{"name":"Key Laboratory of Avian Bioproducts Development, College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonosis, Yangzhou University, Yangzhou 225009, China"},{"name":"Jiangsu Key Laboratory of Zoonosis, Yangzhou University, Yangzhou 225009, China"},{"name":"Joint International Research Laboratory of Agriculture and Agri-Product Safety, The Ministry of Education of China, Yangzhou University, Yangzhou 225009, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,5,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Dever, T.E., Dinman, J.D., and Green, R. (2018). Translation Elongation and Recoding in Eukaryotes. Cold Spring Harb. Perspect. Biol., 10.","DOI":"10.1101\/cshperspect.a032649"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/S0079-6603(08)60889-2","article-title":"Eukaryotic translation elongation factor 1 alpha: Structure, expression, functions, and possible role in aminoacyl-tRNA channeling","volume":"60","author":"Negrutskii","year":"1998","journal-title":"Prog. Nucleic Acid Res. Mol. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"100067","DOI":"10.1016\/j.bbadva.2022.100067","article-title":"The eEF1 family of mammalian translation elongation factors","volume":"3","author":"Negrutskii","year":"2023","journal-title":"BBA Adv."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"9490","DOI":"10.1093\/nar\/gkac685","article-title":"Quaternary organization of the human eEF1B complex reveals unique multi-GEF domain assembly","volume":"50","author":"Bondarchuk","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"22","DOI":"10.2108\/zsj.25.22","article-title":"Roles of three domains of Tetrahymena eEF1A in bundling F-actin","volume":"25","author":"Morita","year":"2008","journal-title":"Zoolog. Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1002\/wrna.1118","article-title":"The many roles of the eukaryotic elongation factor 1 complex","volume":"3","author":"Sasikumar","year":"2012","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.celrep.2013.09.030","article-title":"eEF1A mediates the nuclear export of SNAG-containing proteins via the Exportin5-aminoacyl-tRNA complex","volume":"5","author":"Mingot","year":"2013","journal-title":"Cell Rep."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1002\/jcb.20969","article-title":"Mouse translation elongation factor eEF1A-2 interacts with Prdx-I to protect cells against apoptotic death induced by oxidative stress","volume":"100","author":"Chang","year":"2007","journal-title":"J. Cell. Biochem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e1080","DOI":"10.1038\/cddis.2014.16","article-title":"Blockade of BFA-mediated apoptosis in macrophages by the HIV-1 Nef protein","volume":"5","author":"Abbas","year":"2014","journal-title":"Cell Death Dis."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1038\/sj.cdd.4401078","article-title":"Elongation factor-1 alpha is a selective regulator of growth factor withdrawal and ER stress-induced apoptosis","volume":"9","author":"Talapatra","year":"2002","journal-title":"Cell Death Differ."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1038\/s41419-022-04930-6","article-title":"A novel 3\u2032tRNA-derived fragment tRF-Val promotes proliferation and inhibits apoptosis by targeting EEF1A1 in gastric cancer","volume":"13","author":"Cui","year":"2022","journal-title":"Cell Death Dis."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1111\/cns.12581","article-title":"EF1A1\/HSC70 Cooperatively Suppress Brain Endothelial Cell Apoptosis via Regulating JNK Activity","volume":"22","author":"Liu","year":"2016","journal-title":"CNS Neurosci. Ther."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Abbas, W., Kumar, A., and Herbein, G. (2015). The eEF1A Proteins: At the Crossroads of Oncogenesis, Apoptosis, and Viral Infections. Front. Oncol., 5.","DOI":"10.3389\/fonc.2015.00075"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.neures.2020.03.013","article-title":"Effects of eEF1A2 knockdown on autophagy in an MPP(+)-induced cellular model of Parkinson\u2019s disease","volume":"164","author":"Prommahom","year":"2021","journal-title":"Neurosci. Res."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Xu, B., Liu, L., and Song, G. (2021). Functions and Regulation of Translation Elongation Factors. Front. Mol. Biosci., 8.","DOI":"10.3389\/fmolb.2021.816398"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1016\/S1097-2765(00)00122-2","article-title":"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha","volume":"6","author":"Andersen","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"21209","DOI":"10.1074\/jbc.R110.113795","article-title":"eEF1A: Thinking outside the ribosome","volume":"285","author":"Mateyak","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Mills, A., and Gago, F. (2021). On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22136973"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1016\/j.cell.2016.10.046","article-title":"Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes","volume":"167","author":"Shao","year":"2016","journal-title":"Cell"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Soares, D.C., Barlow, P.N., Newbery, H.J., Porteous, D.J., and Abbott, C.M. (2009). Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0006315"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"24064","DOI":"10.1016\/S0021-9258(18)35946-5","article-title":"Tissue-specific expression in mammalian brain, heart, and muscle of S1, a member of the elongation factor-1 alpha gene family","volume":"267","author":"Lee","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.bbaexp.2006.02.003","article-title":"eEF1B: At the dawn of the 21st century","volume":"1759","author":"Boulben","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1093\/oxfordjournals.jbchem.a122301","article-title":"Peptide elongation factor 1 from yeasts: Purification and biochemical characterization of peptide elongation factors 1 alpha and 1 beta (gamma) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe","volume":"103","author":"Miyazaki","year":"1988","journal-title":"J. Biochem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1093\/oxfordjournals.jbchem.a134348","article-title":"Occurrence of four subunits in high molecular weight forms of polypeptide chain elongation factor 1 from wheat embryo","volume":"94","author":"Ejiri","year":"1983","journal-title":"J. Biochem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1023\/A:1020140527930","article-title":"Multiple phosphorylation sites and quaternary organization of guanine-nucleotide exchange complex of elongation factor-1 (EF-1betagammadelta\/ValRS) control the various functions of EF-1alpha","volume":"18","author":"Minella","year":"1998","journal-title":"Biosci. Rep."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/0014-5793(87)80532-X","article-title":"Primary structure of elongation factor 1 gamma from Artemia","volume":"223","author":"Maessen","year":"1987","journal-title":"FEBS Lett."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"6644","DOI":"10.1093\/nar\/19.23.6644","article-title":"Molecular cloning of Xenopus elongation factor 1 gamma, major M-phase promoting factor substrate","volume":"19","author":"Cormier","year":"1991","journal-title":"Nucleic Acids Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"5907","DOI":"10.1093\/nar\/20.22.5907","article-title":"Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation","volume":"20","author":"Sanders","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2598","DOI":"10.1093\/nar\/20.10.2598","article-title":"Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein L19","volume":"20","author":"Kumabe","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2045","DOI":"10.1002\/pro.5560031117","article-title":"Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling","volume":"3","author":"Koonin","year":"1994","journal-title":"Protein Sci."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1006\/prep.1998.0895","article-title":"Expression, purification, and spectroscopic studies of the guanine nucleotide exchange domain of human elongation factor, EF-1beta","volume":"13","author":"Kriek","year":"1998","journal-title":"Protein Expr. Purif."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/0167-4781(90)90174-Z","article-title":"Elongation factor 1 beta of artemia: Localization of functional sites and homology to elongation factor 1 delta","volume":"1050","author":"Amons","year":"1990","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0378-1119(99)00153-5","article-title":"The elongation factor-1delta (EF-1delta) originates from gene duplication of an EF-1beta ancestor and fusion with a protein-binding domain","volume":"233","author":"Guerrucci","year":"1999","journal-title":"Gene"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0959-437X(05)80275-8","article-title":"Structure of the leucine zipper","volume":"2","author":"Alber","year":"1992","journal-title":"Curr. Opin. Genet. Dev."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2086","DOI":"10.1016\/S0021-9258(17)42139-9","article-title":"Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor (EF) 1 beta gamma delta complex. Essential roles of the NH2-terminal extension of valyl-tRNA synthetase and of the EF-1 delta subunit in complex formation","volume":"269","author":"Bec","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1006\/bbrc.2002.6398","article-title":"Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex","volume":"291","author":"Park","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_37","first-page":"89","article-title":"The protein biosynthesis elongation cycle","volume":"39","author":"Merrick","year":"2000","journal-title":"Cold Spring Harb. Monogr. Arch."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1016\/S0300-9084(97)86738-7","article-title":"Prokaryotic and eukaryotic translation actors: International Union of Biochemistry and Molecular Biology (IUBMB)","volume":"78","author":"Clark","year":"1996","journal-title":"Biochimie"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1128\/MMBR.00059-12","article-title":"The unexpected roles of eukaryotic translation elongation factors in RNA virus replication and pathogenesis","volume":"77","author":"Li","year":"2013","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1016\/0003-9861(84)90310-2","article-title":"Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes","volume":"234","author":"Carvalho","year":"1984","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_41","first-page":"59","article-title":"Structure and function of the eukaryotic ribosome and elongation factors","volume":"48","author":"Taylor","year":"2007","journal-title":"Cold Spring Harb. Monogr. Arch."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"19457","DOI":"10.1074\/jbc.M601076200","article-title":"Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha","volume":"281","author":"Pittman","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1042\/bj20011681","article-title":"Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system","volume":"365","author":"Mansilla","year":"2002","journal-title":"Biochem. J."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/0014-5793(88)80492-7","article-title":"Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor","volume":"238","author":"Wolfson","year":"1988","journal-title":"FEBS Lett."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1038\/347494a0","article-title":"Identification of an actin-binding protein from Dictyostelium as elongation factor 1a","volume":"347","author":"Yang","year":"1990","journal-title":"Nature"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2286","DOI":"10.1016\/S0021-9258(19)39973-9","article-title":"Isolation of an abundant 50,000-dalton actin filament bundling protein from Dictyostelium amoebae","volume":"265","author":"Demma","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"10288","DOI":"10.1074\/jbc.273.17.10288","article-title":"The effect of F-actin on the binding and hydrolysis of guanine nucleotide by Dictyostelium elongation factor 1A","volume":"273","author":"Edmonds","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1083\/jcb.135.4.953","article-title":"F-actin sequesters elongation factor 1alpha from interaction with aminoacyl-tRNA in a pH-dependent reaction","volume":"135","author":"Liu","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1093\/genetics\/157.4.1425","article-title":"Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast","volume":"157","author":"Munshi","year":"2001","journal-title":"Genetics"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"4739","DOI":"10.1074\/jbc.M807945200","article-title":"Coordination of eukaryotic translation elongation factor 1A (eEF1A) function in actin organization and translation elongation by the guanine nucleotide exchange factor eEF1Balpha","volume":"284","author":"Pittman","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/S0304-4165(01)00157-X","article-title":"Elongation factor 1beta is an actin-binding protein","volume":"1527","author":"Furukawa","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1038\/nature04659","article-title":"A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth","volume":"441","author":"Kim","year":"2006","journal-title":"Nature"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1038\/nsmb1301","article-title":"Interaction between the keratin cytoskeleton and eEF1Bgamma affects protein synthesis in epithelial cells","volume":"14","author":"Kim","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2178","DOI":"10.1007\/s00018-003-3201-x","article-title":"Sea urchin elongation factor 1delta (EF1delta) and evidence for cell cycle-directed localization changes of a sub-fraction of the protein at M phase","volume":"60","author":"Boulben","year":"2003","journal-title":"Cell Mol. Life Sci."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"27927","DOI":"10.1074\/jbc.M111.255810","article-title":"Mitotic modulation of translation elongation factor 1 leads to hindered tRNA delivery to ribosomes","volume":"286","author":"Sivan","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"24980","DOI":"10.1074\/jbc.272.40.24980","article-title":"Efficient mammalian protein synthesis requires an intact F-actin system","volume":"272","author":"Stapulionis","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1038\/nrm2818","article-title":"Emerging role for the cytoskeleton as an organizer and regulator of translation","volume":"11","author":"Kim","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"5418","DOI":"10.1074\/jbc.M110685200","article-title":"Peptide elongation factor eEF1A-2\/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis","volume":"277","author":"Ruest","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1042\/BST0371293","article-title":"eEF1A2 and neuronal degeneration","volume":"37","author":"Abbott","year":"2009","journal-title":"Biochem. Soc. Trans."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1002\/hep.22033","article-title":"Etiology-dependent molecular mechanisms in human hepatocarcinogenesis","volume":"47","author":"Schlaeger","year":"2008","journal-title":"Hepatology"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1886","DOI":"10.1002\/hep.26954","article-title":"EEF1A2 inactivates p53 by way of PI3K\/AKT\/mTOR-dependent stabilization of MDM4 in hepatocellular carcinoma","volume":"59","author":"Pellegrino","year":"2014","journal-title":"Hepatology"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1038\/embor.2011.82","article-title":"Transformation of eEF1B\u03b4 into heat-shock response transcription factor by alternative splicing","volume":"12","author":"Kaitsuka","year":"2011","journal-title":"EMBO Rep."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1165\/rcmb.2021-0492OC","article-title":"Prenatal LPS Exposure Promotes Allergic Airway Inflammation via Long Coding RNA NONMMUT033452.2, and Protein Binding Partner, Eef1D","volume":"68","author":"Zhao","year":"2023","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e00239-19","DOI":"10.1128\/JVI.00239-19","article-title":"Oxazole-Benzenesulfonamide Derivatives Inhibit HIV-1 Reverse Transcriptase Interaction with Cellular eEF1A and Reduce Viral Replication","volume":"93","author":"Rawle","year":"2019","journal-title":"J. Virol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.virol.2005.11.031","article-title":"In vivo interaction between Tobacco mosaic virus RNA-dependent RNA polymerase and host translation elongation factor 1A","volume":"347","author":"Yamaji","year":"2006","journal-title":"Virology"},{"key":"ref_66","doi-asserted-by":"crossref","unstructured":"Wei, T., Li, D., Marcial, D., Khan, M., Lin, M.H., Snape, N., Ghildyal, R., Harrich, D., and Spann, K. (2014). The eukaryotic elongation factor 1A is critical for genome replication of the paramyxovirus respiratory syncytial virus. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0114447"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1186\/s12985-018-1091-7","article-title":"The eukaryotic translation elongation factor 1A regulation of actin stress fibers is important for infectious RSV production","volume":"15","author":"Snape","year":"2018","journal-title":"Virol. J."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.virol.2008.11.041","article-title":"Translation elongation factor 1A is a component of the tombusvirus replicase complex and affects the stability of the p33 replication co-factor","volume":"385","author":"Li","year":"2009","journal-title":"Virology"},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Li, Z., Pogany, J., Tupman, S., Esposito, A.M., Kinzy, T.G., and Nagy, P.D. (2010). Translation elongation factor 1A facilitates the assembly of the tombusvirus replicase and stimulates minus-strand synthesis. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001175"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1073\/pnas.69.5.1313","article-title":"Bacteriophage Q replicase contains the protein biosynthesis elongation factors EF Tu and EF Ts","volume":"69","author":"Blumenthal","year":"1972","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1186\/s12985-015-0337-x","article-title":"Binding of the eukaryotic translation elongation factor 1A with the 5\u2032UTR of HIV-1 genomic RNA is important for reverse transcription","volume":"12","author":"Li","year":"2015","journal-title":"Virol. J."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"6433","DOI":"10.1128\/jvi.71.9.6433-6444.1997","article-title":"Translation elongation factor-1 alpha interacts with the 3\u2032 stem-loop region of West Nile virus genomic RNA","volume":"71","author":"Blackwell","year":"1997","journal-title":"J. Virol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"10172","DOI":"10.1128\/JVI.00531-07","article-title":"Interaction between the cellular protein eEF1A and the 3\u2032-terminal stem-loop of West Nile virus genomic RNA facilitates viral minus-strand RNA synthesis","volume":"81","author":"Davis","year":"2007","journal-title":"J. Virol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"4356","DOI":"10.1093\/nar\/26.19.4356","article-title":"Transfer RNA mimicry among tymoviral genomic RNAs ranges from highly efficient to vestigial","volume":"26","author":"Dreher","year":"1998","journal-title":"Nucleic Acids Res."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1002\/j.1460-2075.1986.tb04339.x","article-title":"Interaction of turnip yellow mosaic virus Val-RNA with eukaryotic elongation factor EF-1 [alpha]. Search for a function","volume":"5","author":"Joshi","year":"1986","journal-title":"Embo J."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1074\/jbc.274.2.666","article-title":"Quantitative assessment of EF-1alpha.GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu","volume":"274","author":"Dreher","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.virol.2003.10.028","article-title":"eEF1A binding to aminoacylated viral RNA represses minus strand synthesis by TYMV RNA-dependent RNA polymerase","volume":"321","author":"Matsuda","year":"2004","journal-title":"Virology"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.virol.2003.10.023","article-title":"The tRNA-like structure of Turnip yellow mosaic virus RNA is a 3\u2032-translational enhancer","volume":"321","author":"Matsuda","year":"2004","journal-title":"Virology"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"4563","DOI":"10.3390\/v7082833","article-title":"eEF1A Interacts with the NS5A Protein and Inhibits the Growth of Classical Swine Fever Virus","volume":"7","author":"Li","year":"2015","journal-title":"Viruses"},{"key":"ref_80","unstructured":"Fan, M. (2017). The Effect and Mechanism of Host Factor eEF1A1 on Influenza Virus Propagation. [Master\u2019s Thesis, Huazhong Agricultural University]."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1186\/1743-422X-6-166","article-title":"Analysis of virion associated host proteins in vesicular stomatitis virus using a proteomics approach","volume":"6","author":"Hwang","year":"2009","journal-title":"Virol. J."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"5279","DOI":"10.1128\/JVI.02631-07","article-title":"Proteomics analysis unravels the functional repertoire of coronavirus nonstructural protein 3","volume":"82","author":"Neuman","year":"2008","journal-title":"J. Virol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"5388","DOI":"10.1128\/JVI.73.7.5388-5401.1999","article-title":"Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 Gag polyprotein","volume":"73","author":"Cimarelli","year":"1999","journal-title":"J. Virol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"9039","DOI":"10.1128\/JVI.01013-06","article-title":"Proteomic and biochemical analysis of purified human immunodeficiency virus type 1 produced from infected monocyte-derived macrophages","volume":"80","author":"Chertova","year":"2006","journal-title":"J. Virol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1006\/viro.1999.0075","article-title":"Actin-binding cellular proteins inside human immunodeficiency virus type 1","volume":"266","author":"Ott","year":"2000","journal-title":"Virology"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"2127","DOI":"10.1128\/JVI.80.5.2127-2140.2006","article-title":"Vaccinia virus proteome: Identification of proteins in vaccinia virus intracellular mature virion particles","volume":"80","author":"Chung","year":"2006","journal-title":"J. Virol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.virol.2006.08.025","article-title":"Protein composition of the vaccinia virus mature virion","volume":"358","author":"Resch","year":"2007","journal-title":"Virology"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"11187","DOI":"10.1128\/JVI.78.20.11187-11197.2004","article-title":"Identification of proteins associated with murine cytomegalovirus virions","volume":"78","author":"Kattenhorn","year":"2004","journal-title":"J. Virol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"10960","DOI":"10.1128\/JVI.78.20.10960-10966.2004","article-title":"Identification of proteins in human cytomegalovirus (HCMV) particles: The HCMV proteome","volume":"78","author":"Varnum","year":"2004","journal-title":"J. Virol."},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Gan, H., Zhou, X., Lei, Q., Wu, L., Niu, J., and Zheng, Q. (2024). RNA-dependent RNA polymerase of SARS-CoV-2 regulate host mRNA translation efficiency by hijacking eEF1A factors. Biochim. Biophys. Acta Mol. Basis Dis., 1870.","DOI":"10.1016\/j.bbadis.2023.166871"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"9587","DOI":"10.1073\/pnas.1204673109","article-title":"Eukaryotic elongation factor 1 complex subunits are critical HIV-1 reverse transcription cofactors","volume":"109","author":"Warren","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Wang, Y.E., Park, A., Lake, M., Pentecost, M., Torres, B., Yun, T.E., Wolf, M.C., Holbrook, M.R., Freiberg, A.N., and Lee, B. (2010). Ubiquitin-regulated nuclear-cytoplasmic trafficking of the Nipah virus matrix protein is important for viral budding. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001186"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"2361","DOI":"10.1007\/s00705-016-2903-y","article-title":"Eukaryotic elongation factor 1-beta interacts with the 5\u2032 untranslated region of the M gene of Nipah virus to promote mRNA translation","volume":"161","author":"Uchida","year":"2016","journal-title":"Arch. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"e01391-20","DOI":"10.1128\/JVI.01391-20","article-title":"Eukaryotic Translation Elongation Factor 1 Delta Inhibits the Nuclear Import of the Nucleoprotein and PA-PB1 Heterodimer of Influenza A Virus","volume":"95","author":"Gao","year":"2020","journal-title":"J. Virol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.1128\/JVI.77.4.2359-2368.2003","article-title":"Conserved protein kinases encoded by herpesviruses and cellular protein kinase cdc2 target the same phosphorylation site in eukaryotic elongation factor 1delta","volume":"77","author":"Kawaguchi","year":"2003","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"4456","DOI":"10.1128\/JVI.73.5.4456-4460.1999","article-title":"Cellular elongation factor 1delta is modified in cells infected with representative alpha-, beta-, or gammaherpesviruses","volume":"73","author":"Kawaguchi","year":"1999","journal-title":"J. Virol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1128\/jvi.71.2.1019-1024.1997","article-title":"Interaction of herpes simplex virus 1 alpha regulatory protein ICP0 with elongation factor 1delta: ICP0 affects translational machinery","volume":"71","author":"Kawaguchi","year":"1997","journal-title":"J. Virol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Sammaibashi, S., Yamayoshi, S., and Kawaoka, Y. (2018). Strain-Specific Contribution of Eukaryotic Elongation Factor 1 Gamma to the Translation of Influenza A Virus Proteins. Front. Microbiol., 9.","DOI":"10.3389\/fmicb.2018.01446"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/j.chom.2014.11.002","article-title":"Influenza virus-host interactome screen as a platform for antiviral drug development","volume":"16","author":"Watanabe","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.micpath.2017.09.039","article-title":"eEF1G interaction with foot-and-mouth disease virus nonstructural protein 2B: Identification by yeast two-hybrid system","volume":"112","author":"Zhang","year":"2017","journal-title":"Microb. Pathog."},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Sasvari, Z., Izotova, L., Kinzy, T.G., and Nagy, P.D. (2011). Synergistic roles of eukaryotic translation elongation factors 1B\u03b3 and 1A in stimulation of tombusvirus minus-strand synthesis. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002438"},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Papapanou, M., Papoutsi, E., Giannakas, T., and Katsaounou, P. (2021). Plitidepsin: Mechanisms and Clinical Profile of a Promising Antiviral Agent against COVID-19. J. Pers. Med., 11.","DOI":"10.3390\/jpm11070668"},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Losada, A., Berlanga, J.J., Molina-Guijarro, J.M., Jim\u00e9nez-Ruiz, A., Gago, F., Avil\u00e9s, P., de Haro, C., and Mart\u00ednez-Leal, J.F. (2020). Generation of endoplasmic reticulum stress and inhibition of autophagy by plitidepsin induces proteotoxic apoptosis in cancer cells. Biochem. Pharmacol., 172.","DOI":"10.1016\/j.bcp.2019.113744"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"2640","DOI":"10.1038\/s41467-019-10606-1","article-title":"Structural basis for the inhibition of translation through eIF2\u03b1 phosphorylation","volume":"10","author":"Gordiyenko","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1038\/s41467-025-56151-y","article-title":"Targeting eEF1A reprograms translation and uncovers broad-spectrum antivirals against cap or m(6)A protein synthesis routes","volume":"16","author":"Jarne","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1039\/D0NP00011F","article-title":"Natural products targeting the elongation phase of eukaryotic protein biosynthesis","volume":"37","author":"Sasse","year":"2020","journal-title":"Nat. Prod. Rep."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"402","DOI":"10.37201\/req\/042.2021","article-title":"Plitidepsin, an inhibitor of the cell elongation factor eEF1a, and molnupiravir an analogue of the ribonucleoside cytidine, two new chemical compounds with intense activity against SARS-CoV-2","volume":"34","author":"Reina","year":"2021","journal-title":"Rev. Esp. Quimioter."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1126\/science.abf4058","article-title":"Plitidepsin has potent preclinical efficacy against SARS-CoV-2 by targeting the host protein eEF1A","volume":"371","author":"White","year":"2021","journal-title":"Science"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"105621","DOI":"10.1016\/j.antiviral.2023.105621","article-title":"Anisomycin inhibits Coxsackievirus B replication by promoting the lysosomal degradation of eEF1A1","volume":"215","author":"Shao","year":"2023","journal-title":"Antivir. Res."},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Li, D., Wei, T., Rawle, D.J., Qin, F., Wang, R., Soares, D.C., Jin, H., Sivakumaran, H., Lin, M.H., and Spann, K. (2015). Specific Interaction between eEF1A and HIV RT Is Critical for HIV-1 Reverse Transcription and a Potential Anti-HIV Target. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1005289"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"3999","DOI":"10.1002\/cam4.5250","article-title":"Phase I study of plitidepsin in combination with bortezomib and dexamethasone in patients with relapsed\/refractory multiple myeloma","volume":"12","author":"Mateos","year":"2023","journal-title":"Cancer Med."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"3260","DOI":"10.1158\/1078-0432.CCR-10-0469","article-title":"Phase II clinical and pharmacokinetic study of plitidepsin 3-hour infusion every two weeks alone or with dexamethasone in relapsed and refractory multiple myeloma","volume":"16","author":"Mateos","year":"2010","journal-title":"Clin. Cancer Res."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"2139","DOI":"10.1007\/s00277-019-03739-2","article-title":"Randomized phase III study (ADMYRE) of plitidepsin in combination with dexamethasone vs. dexamethasone alone in patients with relapsed\/refractory multiple myeloma","volume":"98","author":"Spicka","year":"2019","journal-title":"Ann. Hematol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1093\/cid\/ciae227","article-title":"A Phase III Randomized Controlled Trial of Plitidepsin, a Marine-Derived Compound, in Hospitalized Adults with Moderate COVID-19","volume":"79","author":"Landete","year":"2024","journal-title":"Clin. Infect. Dis."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/17\/5\/682\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:28:46Z","timestamp":1760030926000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/17\/5\/682"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5,7]]},"references-count":114,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2025,5]]}},"alternative-id":["v17050682"],"URL":"https:\/\/doi.org\/10.3390\/v17050682","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,5,7]]}}}