{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T12:04:27Z","timestamp":1790078667128,"version":"4.0.1"},"reference-count":145,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2019,1,29]],"date-time":"2019-01-29T00:00:00Z","timestamp":1548720000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>Lassa virus (LASV) is the causative agent of Lassa fever, a human hemorrhagic disease associated with high mortality and morbidity rates, particularly prevalent in West Africa. Over the past few years, a significant amount of novel information has been provided on cellular factors that are determinant elements playing a role in arenavirus multiplication. In this review, we focus on host proteins that intersect with the initial steps of the LASV replication cycle: virus entry and genome replication. A better understanding of relevant virus\u2013host interactions essential for sustaining these critical steps may help to identify possible targets for the rational design of novel therapeutic approaches against LASV and other arenaviruses that cause severe human disease.<\/jats:p>","DOI":"10.3390\/pathogens8010017","type":"journal-article","created":{"date-parts":[[2019,1,29]],"date-time":"2019-01-29T11:27:52Z","timestamp":1548761272000},"page":"17","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["Virus\u2013Host Interactions Involved in Lassa Virus Entry and Genome Replication"],"prefix":"10.3390","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7965-0177","authenticated-orcid":false,"given":"Mar\u00eda Eugenia","family":"Loureiro","sequence":"first","affiliation":[{"name":"Centro de Virolog\u00eda Animal (CEVAN), CONICET-SENASA, Av Sir Alexander Fleming 1653, Mart\u00ednez, Provincia de Buenos Aires B1640CSI, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alejandra","family":"D\u2019Antuono","sequence":"additional","affiliation":[{"name":"Centro de Virolog\u00eda Animal (CEVAN), CONICET-SENASA, Av Sir Alexander Fleming 1653, Mart\u00ednez, Provincia de Buenos Aires B1640CSI, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nora","family":"L\u00f3pez","sequence":"additional","affiliation":[{"name":"Centro de Virolog\u00eda Animal (CEVAN), CONICET-SENASA, Av Sir Alexander Fleming 1653, Mart\u00ednez, Provincia de Buenos Aires B1640CSI, Argentina"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,1,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2295","DOI":"10.1007\/s00705-018-3843-5","article-title":"Taxonomy of the family Arenaviridae and the order Bunyavirales: Update 2018","volume":"163","author":"Maes","year":"2018","journal-title":"Arch. Virol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1007\/s00281-017-0637-x","article-title":"Molecular pathogenesis of viral hemorrhagic fever","volume":"39","author":"Basler","year":"2017","journal-title":"Semin. Immunopathol."},{"key":"ref_3","first-page":"1","article-title":"Lassa fever in West African sub-region: An overview","volume":"44","author":"Ogbu","year":"2007","journal-title":"J. Vector Borne Dis."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Cashman, K.A., Wilkinson, E.R., Zeng, X., Cardile, A.P., Facemire, P.R., Bell, T.M., Bearss, J.J., Shaia, C.I., and Schmaljohn, C.S. (2018). Immune-Mediated Systemic Vasculitis as the Proposed Cause of Sudden-Onset Sensorineural Hearing Loss following Lassa Virus Exposure in Cynomolgus Macaques. mBio, 9.","DOI":"10.1128\/mBio.01896-18"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Mateer, E.J., Huang, C., Shehu, N.Y., and Paessler, S. (2018). Lassa fever-induced sensorineural hearing loss: A neglected public health and social burden. PLoS Negl. Trop. Dis., 12.","DOI":"10.1371\/journal.pntd.0006187"},{"key":"ref_6","unstructured":"Buchmeier, M.J., De la Torre, J.C., and Peters, C.J. (2007). Arenaviridae: The Viruses and Their Replication, Wolters Kluwer Health\/Lippincott Williams & Wilkins."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"16625","DOI":"10.1038\/s41598-017-16875-4","article-title":"Conserved RNA structures in the intergenic regions of ambisense viruses","volume":"7","author":"Kiening","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"5897","DOI":"10.1128\/JVI.00008-06","article-title":"Identification of an N-terminal trimeric coiled-coil core within arenavirus glycoprotein 2 permits assignment to class I viral fusion proteins","volume":"80","author":"Eschli","year":"2006","journal-title":"J. Virol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2162","DOI":"10.3390\/v4102162","article-title":"Envelope glycoprotein of arenaviruses","volume":"4","author":"Burri","year":"2012","journal-title":"Viruses"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.coviro.2018.05.002","article-title":"Lassa virus glycoprotein: Stopping a moving target","volume":"31","author":"Hastie","year":"2018","journal-title":"Curr. Opin. Virol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"13793","DOI":"10.1128\/JVI.78.24.13793-13803.2004","article-title":"Replicon system for Lassa virus","volume":"78","author":"Hass","year":"2004","journal-title":"J. Virol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3470","DOI":"10.1128\/JVI.74.8.3470-3477.2000","article-title":"NP and L proteins of lymphocytic choriomeningitis virus (LCMV) are sufficient for efficient transcription and replication of LCMV genomic RNA analogs","volume":"74","author":"Lee","year":"2000","journal-title":"J. Virol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"12241","DOI":"10.1128\/JVI.75.24.12241-12251.2001","article-title":"Transcription and RNA replication of tacaribe virus genome and antigenome analogs require N and L proteins: Z protein is an inhibitor of these processes","volume":"75","author":"Lopez","year":"2001","journal-title":"J. Virol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"7029","DOI":"10.1128\/JVI.00329-09","article-title":"The RING domain and the L79 residue of Z protein are involved in both the rescue of nucleocapsids and the incorporation of glycoproteins into infectious chimeric arenavirus-like particles","volume":"83","author":"Casabona","year":"2009","journal-title":"J. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"13038","DOI":"10.1128\/JVI.05834-11","article-title":"The C-terminal region of lymphocytic choriomeningitis virus nucleoprotein contains distinct and segregable functional domains involved in NP-Z interaction and counteraction of the type I interferon response","volume":"85","author":"Cheng","year":"2011","journal-title":"J. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"5415","DOI":"10.1128\/JVI.02417-09","article-title":"A role for the C terminus of Mopeia virus nucleoprotein in its incorporation into Z protein-induced virus-like particles","volume":"84","author":"Shtanko","year":"2010","journal-title":"J. Virol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1038\/nature09605","article-title":"Cap binding and immune evasion revealed by Lassa nucleoprotein structure","volume":"468","author":"Qi","year":"2010","journal-title":"Nature"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"19365","DOI":"10.1073\/pnas.1108515108","article-title":"Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding","volume":"108","author":"Hastie","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"12093","DOI":"10.1128\/JVI.00429-11","article-title":"Lassa virus nucleoprotein mutants generated by reverse genetics induce a robust type I interferon response in human dendritic cells and macrophages","volume":"85","author":"Carnec","year":"2011","journal-title":"J. Virol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"13923","DOI":"10.1128\/JVI.01923-14","article-title":"Exonuclease domain of the Lassa virus nucleoprotein is critical to avoid RIG-I signaling and to inhibit the innate immune response","volume":"88","author":"Reynard","year":"2014","journal-title":"J. Virol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"6595","DOI":"10.1128\/JVI.00009-15","article-title":"In vitro and in vivo characterizations of the Pichinde viral NP exoribonuclease function","volume":"89","author":"Huang","year":"2015","journal-title":"J. Virol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"7728","DOI":"10.1128\/JVI.00187-12","article-title":"Arenavirus nucleoprotein targets interferon regulatory factor-activating kinase IKKepsilon","volume":"86","author":"Pythoud","year":"2012","journal-title":"J. Virol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"8185","DOI":"10.1128\/JVI.07240-11","article-title":"Arenavirus nucleoproteins prevent activation of nuclear factor kappa B","volume":"86","author":"Rodrigo","year":"2012","journal-title":"J. Virol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"9452","DOI":"10.1128\/JVI.00155-10","article-title":"Induction and inhibition of type I interferon responses by distinct components of lymphocytic choriomeningitis virus","volume":"84","author":"Zhou","year":"2010","journal-title":"J. Virol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2049","DOI":"10.3390\/v4102049","article-title":"Molecular mechanism of arenavirus assembly and budding","volume":"4","author":"Urata","year":"2012","journal-title":"Viruses"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3390\/pathogens4020283","article-title":"Human hemorrhagic Fever causing arenaviruses: Molecular mechanisms contributing to virus virulence and disease pathogenesis","volume":"4","author":"Shao","year":"2015","journal-title":"Pathogens"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2182","DOI":"10.3390\/v4102182","article-title":"Arenavirus evasion of host anti-viral responses","volume":"4","author":"Hayes","year":"2012","journal-title":"Viruses"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1016\/j.jmb.2018.04.026","article-title":"Novel Insights into Cell Entry of Emerging Human Pathogenic Arenaviruses","volume":"430","author":"Fedeli","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1126\/science.282.5396.2079","article-title":"Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus","volume":"282","author":"Cao","year":"1998","journal-title":"Science"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"5140","DOI":"10.1128\/JVI.76.10.5140-5146.2002","article-title":"New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor","volume":"76","author":"Spiropoulou","year":"2002","journal-title":"J. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Acciani, M., Alston, J.T., Zhao, G., Reynolds, H., Ali, A.M., Xu, B., and Brindley, M. (2017). Mutational analysis of Lassa virus glycoprotein highlights regions required for alpha-dystroglycan utilization. J. Virol., 91.","DOI":"10.1128\/JVI.00574-17"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/S0014-5793(00)01195-9","article-title":"Biosynthesis of dystroglycan: Processing of a precursor propeptide","volume":"468","author":"Holt","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1038\/355696a0","article-title":"Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix","volume":"355","author":"Ervasti","year":"1992","journal-title":"Nature"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1093\/hmg\/2.10.1651","article-title":"Human dystroglycan: Skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization","volume":"2","author":"Milatovich","year":"1993","journal-title":"Hum. Mol. Genet."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1242\/jcs.02814","article-title":"Dystroglycan: From biosynthesis to pathogenesis of human disease","volume":"119","author":"Barresi","year":"2006","journal-title":"J. Cell Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1083\/jcb.122.4.809","article-title":"A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin","volume":"122","author":"Ervasti","year":"1993","journal-title":"J. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"15457","DOI":"10.1074\/jbc.R200031200","article-title":"Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function","volume":"278","author":"Michele","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1016\/0092-8674(91)90035-W","article-title":"Membrane organization of the dystrophin-glycoprotein complex","volume":"66","author":"Ervasti","year":"1991","journal-title":"Cell"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1006\/mcbr.1999.0168","article-title":"WW and EF hand domains of dystrophin-family proteins mediate dystroglycan binding","volume":"2","author":"Chung","year":"1999","journal-title":"Mol. Cell Biol. Res. Commun. MCBRC"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"14297","DOI":"10.1128\/JVI.79.22.14297-14308.2005","article-title":"O Mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function","volume":"79","author":"Imperiali","year":"2005","journal-title":"J. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"14282","DOI":"10.1128\/JVI.79.22.14282-14296.2005","article-title":"Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase LARGE is critical for virus binding","volume":"79","author":"Kunz","year":"2005","journal-title":"J. Virol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1093\/glycob\/cwv021","article-title":"Matriglycan: A novel polysaccharide that links dystroglycan to the basement membrane","volume":"25","author":"Campbell","year":"2015","journal-title":"Glycobiology"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/nsmb.3210","article-title":"Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV","volume":"23","author":"Hastie","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1126\/science.aam7260","article-title":"Structural basis for antibody-mediated neutralization of Lassa virus","volume":"356","author":"Hastie","year":"2017","journal-title":"Science"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"5979","DOI":"10.1128\/JVI.79.10.5979-5987.2005","article-title":"Characterization of the interaction of lassa fever virus with its cellular receptor alpha-dystroglycan","volume":"79","author":"Kunz","year":"2005","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"5685","DOI":"10.1128\/JVI.02574-06","article-title":"Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan\u2019s host-derived ligands","volume":"81","author":"Rojek","year":"2007","journal-title":"J. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/j.cell.2004.06.003","article-title":"Molecular recognition by LARGE is essential for expression of functional dystroglycan","volume":"117","author":"Kanagawa","year":"2004","journal-title":"Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"17426","DOI":"10.1073\/pnas.1114836108","article-title":"Like-acetylglucosaminyltransferase (LARGE)-dependent modification of dystroglycan at Thr-317\/319 is required for laminin binding and arenavirus infection","volume":"108","author":"Hara","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1111\/cmi.12078","article-title":"Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan","volume":"15","author":"Moraz","year":"2013","journal-title":"Cell. Microbiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2713","DOI":"10.1099\/vir.0.2008\/004721-0","article-title":"Post-translational modification of {alpha}-dystroglycan is not critical for lymphocytic choriomeningitis virus receptor function in vivo","volume":"89","author":"Imperiali","year":"2008","journal-title":"J. Gen. Virol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"2067","DOI":"10.1128\/JVI.06451-11","article-title":"Identification of cell surface molecules involved in dystroglycan-independent Lassa virus cell entry","volume":"86","author":"Shimojima","year":"2012","journal-title":"J. Virol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1038\/nri2303","article-title":"Immunobiology of the TAM receptors","volume":"8","author":"Lemke","year":"2008","journal-title":"Nat. Rev. Immunol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"a009076","DOI":"10.1101\/cshperspect.a009076","article-title":"Biology of the TAM receptors","volume":"5","author":"Lemke","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"10109","DOI":"10.1128\/JVI.01157-06","article-title":"Tyro3 family-mediated cell entry of Ebola and Marburg viruses","volume":"80","author":"Shimojima","year":"2006","journal-title":"J. Virol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1016\/j.chom.2012.08.009","article-title":"The TIM and TAM families of phosphatidylserine receptors mediate dengue virus entry","volume":"12","author":"Meertens","year":"2012","journal-title":"Cell Host Microbe"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.celrep.2016.12.045","article-title":"Axl Mediates ZIKA Virus Entry in Human Glial Cells and Modulates Innate Immune Responses","volume":"18","author":"Meertens","year":"2017","journal-title":"Cell Rep."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.chom.2011.03.012","article-title":"The soluble serum protein Gas6 bridges virion envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry","volume":"9","author":"Morizono","year":"2011","journal-title":"Cell Host Microbe"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1126\/science.1155164","article-title":"Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells","volume":"320","author":"Mercer","year":"2008","journal-title":"Science"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/nrmicro3469","article-title":"Viral apoptotic mimicry","volume":"13","author":"Amara","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1038\/nm.1885","article-title":"Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases","volume":"14","author":"Soares","year":"2008","journal-title":"Nat. Med."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Jemielity, S., Wang, J.J., Chan, Y.K., Ahmed, A.A., Li, W., Monahan, S., Bu, X., Farzan, M., Freeman, G.J., and Umetsu, D.T. (2013). TIM-family proteins promote infection of multiple enveloped viruses through virion-associated phosphatidylserine. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003232"},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Fedeli, C., Torriani, G., Galan-Navarro, C., Moraz, M.L., Moreno, H., Gerold, G., and Kunz, S. (2018). Axl Can Serve as Entry Factor for Lassa Virus Depending on the Functional Glycosylation of Dystroglycan. J. Virol., 92.","DOI":"10.1128\/JVI.01613-17"},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Brouillette, R.B., Phillips, E.K., Patel, R., Mahauad-Fernandez, W., Moller-Tank, S., Rogers, K.J., Dillard, J.A., Cooney, A.L., Martinez-Sobrido, L., and Okeoma, C. (2018). TIM-1 Mediates Dystroglycan-Independent Entry of Lassa Virus. J. Virol., 92.","DOI":"10.1128\/JVI.00093-18"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1111\/j.0105-2896.2010.00903.x","article-title":"TIM genes: A family of cell surface phosphatidylserine receptors that regulate innate and adaptive immunity","volume":"235","author":"Freeman","year":"2010","journal-title":"Immunol. Rev."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1016\/j.bbrc.2013.10.106","article-title":"Utilization of human DC-SIGN and L-SIGN for entry and infection of host cells by the New World arenavirus, Junin virus","volume":"441","author":"Martinez","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1111\/tra.12393","article-title":"Differential Use of the C-Type Lectins L-SIGN and DC-SIGN for Phlebovirus Endocytosis","volume":"17","author":"Leger","year":"2016","journal-title":"Traffic"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"6841","DOI":"10.1128\/JVI.76.13.6841-6844.2002","article-title":"C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans","volume":"76","author":"Alvarez","year":"2002","journal-title":"J. Virol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1074\/jbc.M706292200","article-title":"A novel mechanism for LSECtin binding to Ebola virus surface glycoprotein through truncated glycans","volume":"283","author":"Powlesland","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.virol.2005.06.026","article-title":"LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus","volume":"340","author":"Gramberg","year":"2005","journal-title":"Virology"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1007\/s00705-014-2042-2","article-title":"Distinct usage of three C-type lectins by Japanese encephalitis virus: DC-SIGN, DC-SIGNR, and LSECtin","volume":"159","author":"Shimojima","year":"2014","journal-title":"Arch. Virol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"11504","DOI":"10.1128\/JVI.01893-13","article-title":"Role of DC-SIGN in Lassa virus entry into human dendritic cells","volume":"87","author":"Goncalves","year":"2013","journal-title":"J. Virol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2861","DOI":"10.4049\/jimmunol.172.5.2861","article-title":"Lassa virus infection of human dendritic cells and macrophages is productive but fails to activate cells","volume":"172","author":"Baize","year":"2004","journal-title":"J. Immunol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/j.chom.2012.04.017","article-title":"Plasmacytoid dendritic cells are productively infected and activated through TLR-7 early after arenavirus infection","volume":"11","author":"Macal","year":"2012","journal-title":"Cell Host Microbe"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.virol.2008.04.046","article-title":"Lymphocytic choriomeningitis virus uses a novel endocytic pathway for infectious entry via late endosomes","volume":"378","author":"Quirin","year":"2008","journal-title":"Virology"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"7677","DOI":"10.1128\/JVI.00560-08","article-title":"Different mechanisms of cell entry by human-pathogenic Old World and New World arenaviruses","volume":"82","author":"Rojek","year":"2008","journal-title":"J. Virol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"19036","DOI":"10.1073\/pnas.1113643108","article-title":"RNAi screening reveals requirement for host cell secretory pathway in infection by diverse families of negative-strand RNA viruses","volume":"108","author":"Panda","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1128\/JVI.02110-13","article-title":"Sodium hydrogen exchangers contribute to arenavirus cell entry","volume":"88","author":"Iwasaki","year":"2014","journal-title":"J. Virol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"6412","DOI":"10.1128\/JVI.00257-16","article-title":"Lassa Virus Cell Entry via Dystroglycan Involves an Unusual Pathway of Macropinocytosis","volume":"90","author":"Oppliger","year":"2016","journal-title":"J. Virol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1126\/science.1252480","article-title":"Virus entry. Lassa virus entry requires a trigger-induced receptor switch","volume":"344","author":"Jae","year":"2014","journal-title":"Science"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"7584","DOI":"10.1128\/JVI.00651-15","article-title":"Molecular mechanism for LAMP1 recognition by Lassa Virus","volume":"89","author":"Cohen","year":"2015","journal-title":"J. Virol."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Li, S., Sun, Z., Pryce, R., Parsy, M.L., Fehling, S.K., Schlie, K., Siebert, C.A., Garten, W., Bowden, T.A., and Strecker, T. (2016). Acidic pH-Induced conformations and LAMP1 binding of the Lassa Virus glycoprotein spike. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005418"},{"key":"ref_82","doi-asserted-by":"crossref","unstructured":"Hulseberg, C.E., F\u00e9n\u00e9ant, L., Szyma\u0144ska, K.M., and White, J.M. (2018). LAMP1 increases the efficiency of Lassa Virus infection by promoting fusion in less acidic endosomal compartments. MBio, 2.","DOI":"10.1128\/mBio.01818-17"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"10329","DOI":"10.1128\/JVI.01624-16","article-title":"Role of LAMP1 Binding and pH Sensing by the Spike Complex of Lassa Virus","volume":"90","author":"Israeli","year":"2016","journal-title":"J. Virol."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Israeli, H., Cohen-Dvashi, H., Shulman, A., Shimon, A., and Diskin, R. (2017). Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006337"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"King, B.R., Hershkowitz, D., Eisenhauer, P.L., Weir, M.E., Ziegler, C.M., Russo, J., Bruce, E.A., Ballif, B.A., and Botten, J. (2017). A Map of the Arenavirus Nucleoprotein-Host Protein Interactome Reveals that Junin Virus Selectively Impairs the Antiviral Activity of Double-Stranded RNA-Activated Protein Kinase (PKR). J. Virol., 91.","DOI":"10.1128\/JVI.00763-17"},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Ziegler, C.M., Eisenhauer, P., Kelly, J.A., Dang, L.N., Beganovic, V., Bruce, E.A., King, B.R., Shirley, D.J., Weir, M.E., and Ballif, B.A. (2018). A proteomic survey of Junin virus interactions with human proteins reveals host factors required for arenavirus replication. J. Virol., 92.","DOI":"10.1128\/JVI.01565-17"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Khamina, K., Lercher, A., Caldera, M., Schliehe, C., Vilagos, B., Sahin, M., Kosack, L., Bhattacharya, A., Majek, P., and Stukalov, A. (2017). Characterization of host proteins interacting with the lymphocytic choriomeningitis virus L protein. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006758"},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Iwasaki, M., Minder, P., Cai, Y., Kuhn, J.H., Yates, J.R., Torbett, B.E., and de la Torre, J.C. (2018). Interactome analysis of the lymphocytic choriomeningitis virus nucleoprotein in infected cells reveals ATPase Na+\/K+ transporting subunit Alpha 1 and prohibitin as host-cell factors involved in the life cycle of mammarenaviruses. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006892"},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Loureiro, M.E., Zorzetto-Fernandes, A.L., Radoshitzky, S., Chi, X., Dallari, S., Marooki, N., Leger, P., Foscaldi, S., Harjono, V., and Sharma, S. (2018). DDX3 suppresses type I interferons and favors viral replication during Arenavirus infection. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1007125"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.3390\/v4091651","article-title":"Uncovering viral protein-protein interactions and their role in arenavirus life cycle","volume":"4","author":"Loureiro","year":"2012","journal-title":"Viruses"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"9192","DOI":"10.1128\/JVI.00555-06","article-title":"Inhibition of the type I interferon response by the nucleoprotein of the prototypic arenavirus lymphocytic choriomeningitis virus","volume":"80","author":"Zuniga","year":"2006","journal-title":"J. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1991","DOI":"10.1038\/sj.onc.1209239","article-title":"DDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth control","volume":"25","author":"Chang","year":"2006","journal-title":"Oncogene"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"5444","DOI":"10.1128\/MCB.00560-10","article-title":"DDX3 regulates cell growth through translational control of cyclin E1","volume":"30","author":"Lai","year":"2010","journal-title":"Mol. Cell. Biol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1126\/science.1231499","article-title":"RNA helicase DDX3 is a regulatory subunit of casein kinase 1 in Wnt-beta-catenin signaling","volume":"339","author":"Cruciat","year":"2013","journal-title":"Science"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"13922","DOI":"10.1128\/JVI.01517-07","article-title":"DDX3 DEAD-box RNA helicase is required for hepatitis C virus RNA replication","volume":"81","author":"Ariumi","year":"2007","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Lai, M.C., Wang, S.W., Cheng, L., Tarn, W.Y., Tsai, S.J., and Sun, H.S. (2013). Human DDX3 interacts with the HIV-1 Tat protein to facilitate viral mRNA translation. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0068665"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/j.bbrc.2013.04.016","article-title":"Distinct DDX DEAD-box RNA helicases cooperate to modulate the HIV-1 Rev function","volume":"434","author":"Kuroki","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virol.2012.09.041","article-title":"P-body components LSM1, GW182, DDX3, DDX6 and XRN1 are recruited to WNV replication sites and positively regulate viral replication","volume":"436","author":"Chahar","year":"2013","journal-title":"Virology"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.antiviral.2016.04.008","article-title":"Venezuelan equine encephalitis virus non-structural protein 3 (nsP3) interacts with RNA helicases DDX1 and DDX3 in infected cells","volume":"131","author":"Amaya","year":"2016","journal-title":"Antivir. Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1038\/sj.onc.1210687","article-title":"Candidate tumor suppressor DDX3 RNA helicase specifically represses cap-dependent translation by acting as an eIF4E inhibitory protein","volume":"27","author":"Shih","year":"2008","journal-title":"Oncogene"},{"key":"ref_101","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_102","doi-asserted-by":"crossref","unstructured":"Garbelli, A., Beermann, S., Di Cicco, G., Dietrich, U., and Maga, G. (2011). A motif unique to the human DEAD-box protein DDX3 is important for nucleic acid binding, ATP hydrolysis, RNA\/DNA unwinding and HIV-1 replication. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0019810"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"423","DOI":"10.3389\/fgene.2014.00423","article-title":"Multiple functions of DDX3 RNA helicase in gene regulation, tumorigenesis, and viral infection","volume":"5","author":"Ariumi","year":"2014","journal-title":"Front. Genet."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1002\/rmv.1845","article-title":"RNA helicase DDX3: At the crossroad of viral replication and antiviral immunity","volume":"25","author":"Hermoso","year":"2015","journal-title":"Rev. Med. Virol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/ni.3647","article-title":"HIV-1 blocks the signaling adaptor MAVS to evade antiviral host defense after sensing of abortive HIV-1 RNA by the host helicase DDX3","volume":"18","author":"Gringhuis","year":"2017","journal-title":"Nat. Immunol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.bbrc.2014.11.080","article-title":"DEAD-box RNA helicase DDX3X inhibits DENV replication via regulating type one interferon pathway","volume":"456","author":"Li","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Oshiumi, H., Ikeda, M., Matsumoto, M., Watanabe, A., Takeuchi, O., Akira, S., Kato, N., Shimotohno, K., and Seya, T. (2010). Hepatitis C virus core protein abrogates the DDX3 function that enhances IPS-1-mediated IFN-beta induction. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0014258"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2147","DOI":"10.1038\/emboj.2008.143","article-title":"Viral targeting of DEAD box protein 3 reveals its role in TBK1\/IKKepsilon-mediated IRF activation","volume":"27","author":"Schroder","year":"2008","journal-title":"EMBO J."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1038\/emboj.2008.126","article-title":"The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response","volume":"27","author":"Soulat","year":"2008","journal-title":"EMBO J."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"2004","DOI":"10.1128\/MCB.01603-12","article-title":"Human DEAD box helicase 3 couples IkappaB kinase epsilon to interferon regulatory factor 3 activation","volume":"33","author":"Gu","year":"2013","journal-title":"Mol. Cell. Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1042\/BJ20110739","article-title":"Critical roles of RNA helicase DDX3 and its interactions with eIF4E\/PABP1 in stress granule assembly and stress response","volume":"441","author":"Shih","year":"2012","journal-title":"Biochem. J."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"11301","DOI":"10.1128\/JVI.01635-12","article-title":"Arenavirus infection induces discrete cytosolic structures for RNA replication","volume":"86","author":"Baird","year":"2012","journal-title":"J. Virol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"2889","DOI":"10.1099\/vir.0.033407-0","article-title":"Junin virus infection impairs stress-granule formation in Vero cells treated with arsenite via inhibition of eIF2alpha phosphorylation","volume":"92","author":"Linero","year":"2011","journal-title":"J. Gen. Virol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3661","DOI":"10.1128\/JVI.03010-15","article-title":"DDX3 Interacts with Influenza A Virus NS1 and NP Proteins and Exerts Antiviral Function through Regulation of Stress Granule Formation","volume":"90","author":"Liu","year":"2016","journal-title":"J. Virol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"5288","DOI":"10.1128\/JVI.78.10.5288-5298.2004","article-title":"Cellular RNA helicase p68 relocalization and interaction with the hepatitis C virus (HCV) NS5B protein and the potential role of p68 in HCV RNA replication","volume":"78","author":"Goh","year":"2004","journal-title":"J. Virol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2077","DOI":"10.1002\/pmic.200700508","article-title":"Analysis of the interaction of influenza virus polymerase complex with human cell factors","volume":"8","author":"Jorba","year":"2008","journal-title":"Proteomics"},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Bortz, E., Westera, L., Maamary, J., Steel, J., Albrecht, R.A., Manicassamy, B., Chase, G., Martinez-Sobrido, L., Schwemmle, M., and Garcia-Sastre, A. (2011). Host- and strain-specific regulation of influenza virus polymerase activity by interacting cellular proteins. mBio, 16.","DOI":"10.1128\/mBio.00151-11"},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Matkovic, R., Bernard, E., Fontanel, S., Eldin, P., Chazal, N., Hassan Hersi, D., Merits, A., Peloponese, J.M., and Briant, L. (2018). The host DHX9 DExH Box helicase is recruited to Chikungunya virus replication complexes for optimal genomic RNA translation. J. Virol., JVI.01764.","DOI":"10.1128\/JVI.01764-18"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"5384","DOI":"10.1128\/JVI.03216-15","article-title":"Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Protein Interacts with Nsp9 and Cellular DHX9 To Regulate Viral RNA Synthesis","volume":"90","author":"Liu","year":"2016","journal-title":"J. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"11454","DOI":"10.1128\/JVI.01533-08","article-title":"Mapping of the tacaribe arenavirus Z-protein binding sites on the L protein identified both amino acids within the putative polymerase domain and a region at the N terminus of L that are critically involved in binding","volume":"82","author":"Wilda","year":"2008","journal-title":"J. Virol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"20069","DOI":"10.1073\/pnas.1007152107","article-title":"Assembly of a functional Machupo virus polymerase complex","volume":"107","author":"Kranzusch","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Morin, B., Coutard, B., Lelke, M., Ferron, F., Kerber, R., Jamal, S., Frangeul, A., Baronti, C., Charrel, R., and de Lamballerie, X. (2010). The N-terminal domain of the arenavirus L protein is an RNA endonuclease essential in mRNA transcription. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001038"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1128\/JVI.00721-10","article-title":"Domain structure of Lassa virus L protein","volume":"85","author":"Brunotte","year":"2011","journal-title":"J. Virol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.sbi.2016.01.002","article-title":"Towards a structural understanding of RNA synthesis by negative strand RNA viral polymerases","volume":"36","author":"Reguera","year":"2016","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.virusres.2017.01.018","article-title":"Transcription and replication mechanisms of Bunyaviridae and Arenaviridae L proteins","volume":"234","author":"Ferron","year":"2017","journal-title":"Virus Res."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1016\/j.cell.2015.05.006","article-title":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter","volume":"161","author":"Gerlach","year":"2015","journal-title":"Cell"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"7262","DOI":"10.1128\/JVI.79.11.7262-7268.2005","article-title":"Genetic and biochemical evidence for an oligomeric structure of the functional L polymerase of the prototypic arenavirus lymphocytic choriomeningitis virus","volume":"79","author":"Sanchez","year":"2005","journal-title":"J. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1016\/j.molcel.2014.12.031","article-title":"Cryo-EM structure of influenza virus RNA polymerase complex at 4.3 A resolution","volume":"57","author":"Chang","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/j.virol.2015.03.018","article-title":"The RNA synthesis machinery of negative-stranded RNA viruses","volume":"479\u2013480","author":"Ortin","year":"2015","journal-title":"Virology"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1099\/vir.0.030163-0","article-title":"Differential effect of acute and persistent Junin virus infections on the nucleo-cytoplasmic trafficking and expression of heterogeneous nuclear ribonucleoproteins type A and B","volume":"92","author":"Maeto","year":"2011","journal-title":"J. Gen. Virol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.virusres.2015.04.001","article-title":"The heterogeneous nuclear ribonucleoprotein K (hnRNP K) is a host factor required for dengue virus and Junin virus multiplication","volume":"203","author":"Brunetti","year":"2015","journal-title":"Virus Res."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Chang, C.K., Chen, C.J., Wu, C.C., Chen, S.W., Shih, S.R., and Kuo, R.L. (2017). Cellular hnRNP A2\/B1 interacts with the NP of influenza A virus and impacts viral replication. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0188214"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1111\/j.1600-0854.2006.00461.x","article-title":"Trafficking of HIV-1 RNA is mediated by heterogeneous nuclear ribonucleoprotein A2 expression and impacts on viral assembly","volume":"7","author":"Levesque","year":"2006","journal-title":"Traffic"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"10059","DOI":"10.1128\/JVI.01257-13","article-title":"Heterogeneous nuclear ribonucleoprotein K supports vesicular stomatitis virus replication by regulating cell survival and cellular gene expression","volume":"87","author":"Dinh","year":"2013","journal-title":"J. Virol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"10700","DOI":"10.1128\/JVI.77.19.10700-10705.2003","article-title":"Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles [corrected]","volume":"77","author":"Strecker","year":"2003","journal-title":"J. Virol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2973","DOI":"10.3390\/v4112973","article-title":"Multifunctional nature of the arenavirus RING finger protein Z","volume":"4","author":"Fehling","year":"2012","journal-title":"Viruses"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"12304","DOI":"10.1128\/JVI.05691-11","article-title":"Molecular determinants of arenavirus Z protein homo-oligomerization and L polymerase binding","volume":"85","author":"Loureiro","year":"2011","journal-title":"J. Virol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"19743","DOI":"10.1073\/pnas.1112742108","article-title":"Arenavirus Z protein controls viral RNA synthesis by locking a polymerase-promoter complex","volume":"108","author":"Kranzusch","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"12625","DOI":"10.1074\/jbc.M510596200","article-title":"Association of RNA helicase a with human immunodeficiency virus type 1 particles","volume":"281","author":"Roy","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_140","unstructured":"WHO (2019, January 28). List of Blueprint Priority Diseases. Available online: https:\/\/www.who.int\/blueprint\/priority-diseases\/en\/."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1056\/NEJM198601023140104","article-title":"Lassa fever. Effective therapy with ribavirin","volume":"314","author":"McCormick","year":"1986","journal-title":"N. Engl. J. Med."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"14775","DOI":"10.1038\/srep14775","article-title":"The broad-spectrum antiviral favipiravir protects guinea pigs from lethal Lassa virus infection post-disease onset","volume":"12","author":"Safronetz","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1093\/cid\/cix406","article-title":"Favipiravir and Ribavirin Treatment of Epidemiologically Linked Cases of Lassa Fever","volume":"1","author":"Raabe","year":"2017","journal-title":"Clin. Infect. Dis."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/JVI.01902-16","article-title":"Lassa Virus Cell Entry Reveals New Aspects of Virus-Host Cell Interaction","volume":"91","author":"Torriani","year":"2017","journal-title":"J. Virol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"5388","DOI":"10.1073\/pnas.1522987113","article-title":"Human DDX3 protein is a valuable target to develop broad spectrum antiviral agents","volume":"113","author":"Brai","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-0817\/8\/1\/17\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T12:29:25Z","timestamp":1760185765000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-0817\/8\/1\/17"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,1,29]]},"references-count":145,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2019,3]]}},"alternative-id":["pathogens8010017"],"URL":"https:\/\/doi.org\/10.3390\/pathogens8010017","relation":{},"ISSN":["2076-0817"],"issn-type":[{"value":"2076-0817","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,1,29]]}}}