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dc.contributor.authorSerquina, Anna Kristina
dc.contributor.authorDas, Suman R.
dc.contributor.authorPopova, Elena
dc.contributor.authorOjelabi, Ogooluwa A.
dc.contributor.authorRoy, Christian K.
dc.contributor.authorGottlinger, Heinrich G.
dc.date2022-08-11T08:08:55.000
dc.date.accessioned2022-08-23T16:11:59Z
dc.date.available2022-08-23T16:11:59Z
dc.date.issued2013-08-01
dc.date.submitted2013-06-27
dc.identifier.citationSerquiña AK, Das SR, Popova E, Ojelabi OA, Roy CK, Göttlinger HG. UPF1 is crucial for the infectivity of human immunodeficiency virus type 1 progeny virions. J Virol. 2013 Aug;87(16):8853-61. doi: 10.1128/JVI.00925-13. <a href="http://dx.doi.org/10.1128/JVI.00925-13">Link to article on publisher's website</a>
dc.identifier.issn1098-5514
dc.identifier.doi10.1128/JVI.00925-13
dc.identifier.pmid23785196
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33298
dc.description.abstractThe SF1 helicase MOV10 is an antiviral factor that is incorporated into human immunodeficiency virus type 1 (HIV-1) virions. We now report that HIV-1 virions also incorporate UPF1, which belongs to the same SF1 helicase subfamily as MOV10 and functions in the nonsense-mediated decay (NMD) pathway. Unlike ectopic MOV10, the overexpression of UPF1 does not impair the infectivity of HIV-1 progeny virions. However, UPF1 becomes a potent inhibitor of HIV-1 progeny virion infectivity when residues required for its helicase activity are mutated. In contrast, equivalent mutations abolish the antiviral activity of MOV10. Importantly, cells depleted of endogenous UPF1, but not of another NMD core component, produce HIV-1 virions of substantially lower specific infectivity. The defect is at the level of reverse transcription, the same stage of the HIV-1 life cycle inhibited by ectopic MOV10. Thus, whereas ectopic MOV10 restricts HIV-1 replication, the related UPF1 helicase functions as a cofactor at an early post-entry step.
dc.language.isoen_US
dc.publisherAmerican Society For Microbiology
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=23785196&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1128/JVI.00925-13
dc.subjectRNA Helicases; Nonsense Mediated mRNA Decay; HIV-1; Virion
dc.subjectImmunology of Infectious Disease
dc.subjectVirology
dc.titleUPF1 is Crucial for the Infectivity of Human Immunodeficiency Virus type 1 Progeny Virions
dc.typeJournal Article
dc.source.journaltitleJournal of virology
dc.source.volume87
dc.source.issue16
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1828
dc.identifier.contextkey4263681
html.description.abstract<p>The SF1 helicase MOV10 is an antiviral factor that is incorporated into human immunodeficiency virus type 1 (HIV-1) virions. We now report that HIV-1 virions also incorporate UPF1, which belongs to the same SF1 helicase subfamily as MOV10 and functions in the nonsense-mediated decay (NMD) pathway. Unlike ectopic MOV10, the overexpression of UPF1 does not impair the infectivity of HIV-1 progeny virions. However, UPF1 becomes a potent inhibitor of HIV-1 progeny virion infectivity when residues required for its helicase activity are mutated. In contrast, equivalent mutations abolish the antiviral activity of MOV10. Importantly, cells depleted of endogenous UPF1, but not of another NMD core component, produce HIV-1 virions of substantially lower specific infectivity. The defect is at the level of reverse transcription, the same stage of the HIV-1 life cycle inhibited by ectopic MOV10. Thus, whereas ectopic MOV10 restricts HIV-1 replication, the related UPF1 helicase functions as a cofactor at an early post-entry step.</p>
dc.identifier.submissionpathgsbs_sp/1828
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentProgram in Gene Function and Expression
dc.source.pages8853-61
dc.contributor.studentAnna Kristina Serquina


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