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  1. AU=St Gelais Corine
  2. AU=Engstrom Malitta
  3. AU="Hongo, Akane"
  4. AU="Krykorková, I"
  5. AU=Yan Bing
  6. AU="Nakos, Konstantinos"
  7. AU="Schreiner, Ryan"
  8. AU=Pltz T
  9. AU="Akhmanova, Anna" AU="Akhmanova, Anna"
  10. AU="Goretsky, Anton"
  11. AU="Cordoza, Makayla L"
  12. AU=Midoux Patrick AU=Midoux Patrick
  13. AU="Mundt, H M"
  14. AU=Tsivitse Susan

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  1. Artikel ; Online: Human lysyl-tRNA synthetase phosphorylation promotes HIV-1 proviral DNA transcription.

    Tang, Yingke / Behrens, Ryan T / St Gelais, Corine / Wu, Siqi / Vivekanandan, Saravanan / Razin, Ehud / Fang, Pengfei / Wu, Li / Sherer, Nathan / Musier-Forsyth, Karin

    Nucleic acids research

    2023  Band 51, Heft 22, Seite(n) 12111–12123

    Abstract: Human lysyl-tRNA synthetase (LysRS) was previously shown to be re-localized from its normal cytoplasmic location in a multi-aminoacyl-tRNA synthetase complex (MSC) to the nucleus of HIV-1 infected cells. Nuclear localization depends on S207 ... ...

    Abstract Human lysyl-tRNA synthetase (LysRS) was previously shown to be re-localized from its normal cytoplasmic location in a multi-aminoacyl-tRNA synthetase complex (MSC) to the nucleus of HIV-1 infected cells. Nuclear localization depends on S207 phosphorylation but the nuclear function of pS207-LysRS in the HIV-1 lifecycle is unknown. Here, we show that HIV-1 replication was severely reduced in a S207A-LysRS knock-in cell line generated by CRISPR/Cas9; this effect was rescued by S207D-LysRS. LysRS phosphorylation up-regulated HIV-1 transcription, as did direct transfection of Ap4A, an upstream transcription factor 2 (USF2) activator that is synthesized by pS207-LysRS. Overexpressing an MSC-derived peptide known to stabilize LysRS MSC binding inhibited HIV-1 replication. Transcription of HIV-1 proviral DNA and other USF2 target genes was reduced in peptide-expressing cells. We propose that nuclear pS207-LysRS generates Ap4A, leading to activation of HIV-1 transcription. Our results suggest a new role for nuclear LysRS in facilitating HIV-1 replication and new avenues for antiviral therapy.
    Mesh-Begriff(e) Humans ; DNA/metabolism ; HIV-1/physiology ; Lysine-tRNA Ligase/metabolism ; Peptides/metabolism ; Phosphorylation ; Proviruses/metabolism ; Cell Nucleus/metabolism ; Cell Nucleus/virology ; Virus Replication
    Chemische Substanzen DNA (9007-49-2) ; Lysine-tRNA Ligase (EC 6.1.1.6) ; Peptides
    Sprache Englisch
    Erscheinungsdatum 2023-11-07
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkad941
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: The Dynamic Interplay between HIV-1, SAMHD1, and the Innate Antiviral Response.

    Antonucci, Jenna M / St Gelais, Corine / Wu, Li

    Frontiers in immunology

    2017  Band 8, Seite(n) 1541

    Abstract: The innate immune response constitutes the first cellular line of defense against initial HIV-1 infection. Immune cells sense invading virus and trigger signaling cascades that induce antiviral defenses to control or eliminate infection. Professional ... ...

    Abstract The innate immune response constitutes the first cellular line of defense against initial HIV-1 infection. Immune cells sense invading virus and trigger signaling cascades that induce antiviral defenses to control or eliminate infection. Professional antigen-presenting cells located in mucosal tissues, including dendritic cells and macrophages, are critical for recognizing HIV-1 at the site of initial exposure. These cells are less permissive to HIV-1 infection compared to activated CD4
    Sprache Englisch
    Erscheinungsdatum 2017
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Review
    ZDB-ID 2606827-8
    ISSN 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2017.01541
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: TRAF6 and TAK1 Contribute to SAMHD1-Mediated Negative Regulation of NF-κB Signaling.

    Espada, Constanza E / St Gelais, Corine / Bonifati, Serena / Maksimova, Victoria V / Cahill, Michael P / Kim, Sun Hee / Wu, Li

    Journal of virology

    2021  Band 95, Heft 3

    Abstract: Sterile alpha motif and HD domain-containing protein 1 (SAMHD1) restricts HIV-1 replication by limiting the intracellular deoxynucleoside triphosphate (dNTP) pool. SAMHD1 also suppresses the activation of NF-κB in response to viral infections and ... ...

    Abstract Sterile alpha motif and HD domain-containing protein 1 (SAMHD1) restricts HIV-1 replication by limiting the intracellular deoxynucleoside triphosphate (dNTP) pool. SAMHD1 also suppresses the activation of NF-κB in response to viral infections and inflammatory stimuli. However, the mechanisms by which SAMHD1 negatively regulates this pathway remain unclear. Here, we show that SAMHD1-mediated suppression of NF-κB activation is modulated by two key mediators of NF-κB signaling, tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and transforming growth factor β-activated kinase 1 (TAK1). We compared NF-κB activation stimulated by interleukin (IL)-1β in monocytic THP-1 control and SAMHD1 knockout (KO) cells with and without partial TRAF6 knockdown (KD), or in cells treated with TAK1 inhibitors. Relative to control cells, IL-1β-treated SAMHD1 KO cells showed increased phosphorylation of the inhibitor of NF-κB (IκBα), an indication of pathway activation, and elevated levels of TNF-α mRNA. Moreover, SAMHD1 KO combined with TRAF6 KD or pharmacological TAK1 inhibition reduced IκBα phosphorylation and TNF-α mRNA to the level of control cells. SAMHD1 KO cells infected with single-cycle HIV-1 showed elevated infection and TNF-α mRNA levels compared to control cells, and the effects were significantly reduced by TRAF6 KD or TAK1 inhibition. We further demonstrated that overexpressed SAMHD1 inhibited TRAF6-stimulated NF-κB reporter activity in HEK293T cells in a dose-dependent manner. SAMHD1 contains a nuclear localization signal (NLS), but an NLS-defective SAMHD1 exhibited a suppressive effect similar to the wild-type protein. Our data suggest that the TRAF6-TAK1 axis contributes to SAMHD1-mediated suppression of NF-κB activation and HIV-1 infection.
    Mesh-Begriff(e) Gene Expression Regulation ; HEK293 Cells ; HIV Infections/immunology ; HIV Infections/metabolism ; HIV Infections/virology ; HIV-1/physiology ; Humans ; Immunity, Innate/immunology ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; MAP Kinase Kinase Kinases/genetics ; MAP Kinase Kinase Kinases/metabolism ; NF-kappa B/genetics ; NF-kappa B/metabolism ; SAM Domain and HD Domain-Containing Protein 1/genetics ; SAM Domain and HD Domain-Containing Protein 1/metabolism ; Signal Transduction
    Chemische Substanzen Intracellular Signaling Peptides and Proteins ; NF-kappa B ; Tifab protein, human ; MAP Kinase Kinase Kinases (EC 2.7.11.25) ; MAP kinase kinase kinase 7 (EC 2.7.11.25) ; SAM Domain and HD Domain-Containing Protein 1 (EC 3.1.5.-) ; SAMHD1 protein, human (EC 3.1.5.-)
    Sprache Englisch
    Erscheinungsdatum 2021-01-13
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.01970-20
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: SAMHD1 Suppression of Antiviral Immune Responses.

    Chen, Shuliang / Bonifati, Serena / Qin, Zhihua / St Gelais, Corine / Wu, Li

    Trends in microbiology

    2018  Band 27, Heft 3, Seite(n) 254–267

    Abstract: SAMHD1 is a host triphosphohydrolase that degrades intracellular deoxynucleoside triphosphates (dNTPs) to a lower level that restricts viral DNA synthesis, and thus prevents replication of diverse viruses in nondividing cells. Recent progress indicates ... ...

    Abstract SAMHD1 is a host triphosphohydrolase that degrades intracellular deoxynucleoside triphosphates (dNTPs) to a lower level that restricts viral DNA synthesis, and thus prevents replication of diverse viruses in nondividing cells. Recent progress indicates that SAMHD1 negatively regulates antiviral innate immune responses and inflammation through interacting with various key proteins in immune signaling and DNA damage-repair pathways. SAMHD1 can also modulate antibody production in adaptive immune responses. In this review, we summarize how SAMHD1 regulates antiviral immune responses through distinct mechanisms, and discuss the implications of these new functions of SAMHD1. Furthermore, we propose important new questions and future directions that can advance functional and mechanistic studies of SAMHD1-mediated immune regulation during viral infections.
    Mesh-Begriff(e) Animals ; Gene Expression Regulation/immunology ; HIV Infections/immunology ; Humans ; Immunity, Innate ; Mice ; SAM Domain and HD Domain-Containing Protein 1/genetics ; SAM Domain and HD Domain-Containing Protein 1/immunology ; Signal Transduction/immunology ; Virus Replication/immunology
    Chemische Substanzen SAM Domain and HD Domain-Containing Protein 1 (EC 3.1.5.-)
    Sprache Englisch
    Erscheinungsdatum 2018-10-15
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1158963-2
    ISSN 1878-4380 ; 0966-842X
    ISSN (online) 1878-4380
    ISSN 0966-842X
    DOI 10.1016/j.tim.2018.09.009
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Non-POU Domain-Containing Octamer-Binding Protein Negatively Regulates HIV-1 Infection in CD4(+) T Cells.

    St Gelais, Corine / Roger, Jonathan / Wu, Li

    AIDS research and human retroviruses

    2015  Band 31, Heft 8, Seite(n) 806–816

    Abstract: HIV-1 interacts with numerous cellular proteins during viral replication. Identifying such host proteins and characterizing their roles in HIV-1 infection can deepen our understanding of the dynamic interplay between host and pathogen. We previously ... ...

    Abstract HIV-1 interacts with numerous cellular proteins during viral replication. Identifying such host proteins and characterizing their roles in HIV-1 infection can deepen our understanding of the dynamic interplay between host and pathogen. We previously identified non-POU domain-containing octamer-binding protein (NonO or p54nrb) as one of host factors associated with catalytically active preintegration complexes (PIC) of HIV-1 in infected CD4(+) T cells. NonO is involved in nuclear processes including transcriptional regulation and RNA splicing. Although NonO has been identified as an HIV-1 interactant in several recent studies, its role in HIV-1 replication has not been characterized. We investigated the effect of NonO on the HIV-1 life cycle in CD4(+) T cell lines and primary CD4(+) T cells using single-cycle and replication-competent HIV-1 infection assays. We observed that short hairpin RNA (shRNA)-mediated stable NonO knockdown in a CD4(+) Jurkat T cell line and primary CD4(+) T cells did not affect cell viability or proliferation, but enhanced HIV-1 infection. The enhancement of HIV-1 infection in Jurkat T cells correlated with increased viral reverse transcription and gene expression. Knockdown of NonO expression in Jurkat T cells modestly enhanced HIV-1 gag mRNA expression and Gag protein synthesis, suggesting that viral gene expression and RNA regulation are the predominantly affected events causing enhanced HIV-1 replication in NonO knockdown (KD) cells. Furthermore, overexpression of NonO in Jurkat T cells reduced HIV-1 single-cycle infection by 41% compared to control cells. Our data suggest that NonO negatively regulates HIV-1 infection in CD4(+) T cells, albeit it has modest effects on early and late stages of the viral life cycle, highlighting the importance of host proteins associated with HIV-1 PIC in regulating viral replication.
    Mesh-Begriff(e) CD4-Positive T-Lymphocytes/immunology ; CD4-Positive T-Lymphocytes/virology ; Cells, Cultured ; Gene Knockdown Techniques ; HIV-1/immunology ; HIV-1/physiology ; Host-Pathogen Interactions ; Humans ; Nuclear Matrix-Associated Proteins/antagonists & inhibitors ; Nuclear Matrix-Associated Proteins/metabolism ; Octamer Transcription Factors/antagonists & inhibitors ; Octamer Transcription Factors/metabolism ; RNA-Binding Proteins/antagonists & inhibitors ; RNA-Binding Proteins/metabolism ; Virus Replication
    Chemische Substanzen NONO protein, human ; Nuclear Matrix-Associated Proteins ; Octamer Transcription Factors ; RNA-Binding Proteins
    Sprache Englisch
    Erscheinungsdatum 2015-08
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 639130-8
    ISSN 1931-8405 ; 0889-2229
    ISSN (online) 1931-8405
    ISSN 0889-2229
    DOI 10.1089/AID.2014.0313
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: SAMHD1: a new insight into HIV-1 restriction in myeloid cells.

    St Gelais, Corine / Wu, Li

    Retrovirology

    2011  Band 8, Seite(n) 55

    Abstract: Human myeloid-lineage cells are refractory to HIV-1 infection. The Vpx proteins from HIV-2 and sooty mangabey SIV render these cells permissive to HIV-1 infection through proteasomal degradation of a putative restriction factor. Two recent studies ... ...

    Abstract Human myeloid-lineage cells are refractory to HIV-1 infection. The Vpx proteins from HIV-2 and sooty mangabey SIV render these cells permissive to HIV-1 infection through proteasomal degradation of a putative restriction factor. Two recent studies discovered the cellular protein SAMHD1 to be this restriction factor, demonstrating that Vpx induces proteasomal degradation of SAMHD1 and enhances HIV-1 infection in myeloid-lineage cells. SAMHD1 functions as a myeloid-cell-specific HIV-1 restriction factor by inhibiting viral DNA synthesis. Here we discuss the implications of these findings in delineating the mechanisms of HIV-1 restriction in myeloid-lineage cells and the potential role of Vpx in lentiviral pathogenesis.
    Mesh-Begriff(e) HIV-1/growth & development ; HIV-1/immunology ; Humans ; Models, Biological ; Monomeric GTP-Binding Proteins/immunology ; Monomeric GTP-Binding Proteins/metabolism ; Myeloid Cells/immunology ; Myeloid Cells/virology ; SAM Domain and HD Domain-Containing Protein 1
    Chemische Substanzen SAM Domain and HD Domain-Containing Protein 1 (EC 3.1.5.-) ; SAMHD1 protein, human (EC 3.1.5.-) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2)
    Sprache Englisch
    Erscheinungsdatum 2011-07-08
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ISSN 1742-4690
    ISSN (online) 1742-4690
    DOI 10.1186/1742-4690-8-55
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel: SAMHD1 Suppression of Antiviral Immune Responses

    Chen, Shuliang / Bonifati, Serena / Qin, Zhihua / St. Gelais, Corine / Wu, Li

    Trends in microbiology. 2019 Mar., v. 27, no. 3

    2019  

    Abstract: SAMHD1 is a host triphosphohydrolase that degrades intracellular deoxynucleoside triphosphates (dNTPs) to a lower level that restricts viral DNA synthesis, and thus prevents replication of diverse viruses in nondividing cells. Recent progress indicates ... ...

    Abstract SAMHD1 is a host triphosphohydrolase that degrades intracellular deoxynucleoside triphosphates (dNTPs) to a lower level that restricts viral DNA synthesis, and thus prevents replication of diverse viruses in nondividing cells. Recent progress indicates that SAMHD1 negatively regulates antiviral innate immune responses and inflammation through interacting with various key proteins in immune signaling and DNA damage-repair pathways. SAMHD1 can also modulate antibody production in adaptive immune responses. In this review, we summarize how SAMHD1 regulates antiviral immune responses through distinct mechanisms, and discuss the implications of these new functions of SAMHD1. Furthermore, we propose important new questions and future directions that can advance functional and mechanistic studies of SAMHD1-mediated immune regulation during viral infections.
    Schlagwörter DNA ; DNA replication ; adaptive immunity ; antibody formation ; enzymes ; inflammation ; innate immunity ; proteins ; viruses
    Sprache Englisch
    Erscheinungsverlauf 2019-03
    Umfang p. 254-267.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 1158963-2
    ISSN 1878-4380 ; 0966-842X
    ISSN (online) 1878-4380
    ISSN 0966-842X
    DOI 10.1016/j.tim.2018.09.009
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  8. Artikel ; Online: N

    Lu, Wuxun / Tirumuru, Nagaraja / St Gelais, Corine / Koneru, Pratibha C / Liu, Chang / Kvaratskhelia, Mamuka / He, Chuan / Wu, Li

    The Journal of biological chemistry

    2018  Band 293, Heft 34, Seite(n) 12992–13005

    Abstract: ... The ... ...

    Abstract The internal
    Mesh-Begriff(e) Adenosine/analogs & derivatives ; Adenosine/metabolism ; Gene Products, gag/metabolism ; HIV Infections/metabolism ; HIV Infections/virology ; HIV-1/growth & development ; HIV-1/metabolism ; HeLa Cells ; Humans ; Protein Binding ; RNA, Viral/metabolism ; RNA-Binding Proteins/metabolism ; Virion/growth & development ; Virion/metabolism ; Virus Internalization
    Chemische Substanzen Gene Products, gag ; RNA, Viral ; RNA-Binding Proteins ; YTHDF1 protein, human ; YTHDF2 protein, human ; YTHDF3 protein, human ; N-methyladenosine (CLE6G00625) ; Adenosine (K72T3FS567)
    Sprache Englisch
    Erscheinungsdatum 2018-07-05
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA118.004215
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel ; Online: SAMHD1

    Wu Li / St Gelais Corine

    Retrovirology, Vol 8, Iss 1, p

    a new insight into HIV-1 restriction in myeloid cells

    2011  Band 55

    Abstract: Abstract Human myeloid-lineage cells are refractory to HIV-1 infection. The Vpx proteins from HIV-2 and sooty mangabey SIV render these cells permissive to HIV-1 infection through proteasomal degradation of a putative restriction factor. Two recent ... ...

    Abstract Abstract Human myeloid-lineage cells are refractory to HIV-1 infection. The Vpx proteins from HIV-2 and sooty mangabey SIV render these cells permissive to HIV-1 infection through proteasomal degradation of a putative restriction factor. Two recent studies discovered the cellular protein SAMHD1 to be this restriction factor, demonstrating that Vpx induces proteasomal degradation of SAMHD1 and enhances HIV-1 infection in myeloid-lineage cells. SAMHD1 functions as a myeloid-cell-specific HIV-1 restriction factor by inhibiting viral DNA synthesis. Here we discuss the implications of these findings in delineating the mechanisms of HIV-1 restriction in myeloid-lineage cells and the potential role of Vpx in lentiviral pathogenesis.
    Schlagwörter Medicine (General) ; R5-920 ; Medicine ; R ; DOAJ:Medicine (General) ; DOAJ:Health Sciences ; Immunologic diseases. Allergy ; RC581-607
    Sprache Englisch
    Erscheinungsdatum 2011-07-01T00:00:00Z
    Verlag BioMed Central
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  10. Artikel ; Online: HIV-1 Exploits a Dynamic Multi-aminoacyl-tRNA Synthetase Complex To Enhance Viral Replication.

    Duchon, Alice A / St Gelais, Corine / Titkemeier, Nathan / Hatterschide, Joshua / Wu, Li / Musier-Forsyth, Karin

    Journal of virology

    2017  Band 91, Heft 21

    Abstract: A hallmark of retroviruses such as human immunodeficiency virus type 1 (HIV-1) is reverse transcription of genomic RNA to DNA, a process that is primed by cellular tRNAs. HIV-1 recruits human ... ...

    Abstract A hallmark of retroviruses such as human immunodeficiency virus type 1 (HIV-1) is reverse transcription of genomic RNA to DNA, a process that is primed by cellular tRNAs. HIV-1 recruits human tRNA
    Mesh-Begriff(e) Amino Acyl-tRNA Synthetases/metabolism ; Cytoplasm/metabolism ; HEK293 Cells ; HIV Infections/metabolism ; HIV Infections/virology ; HIV-1/physiology ; Humans ; Lysine-tRNA Ligase/metabolism ; RNA, Transfer, Lys/metabolism ; Virus Assembly ; Virus Replication
    Chemische Substanzen RNA, Transfer, Lys ; Amino Acyl-tRNA Synthetases (EC 6.1.1.-) ; Lysine-tRNA Ligase (EC 6.1.1.6)
    Sprache Englisch
    Erscheinungsdatum 2017-10-13
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.01240-17
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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