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Book ; Online ; Thesis: Human host factors involved in HIV-1 replication

Hain, Anika [Verfasser] / Münk, Carsten [Gutachter]

2017

Author's details	Anika Hain ; Gutachter: Carsten Münk
Keywords	Biowissenschaften, Biologie ; Life Science, Biology
Subject code	sg570
Language	English
Publisher	Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf
Publishing place	Düsseldorf
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: IL-2 Inducible Kinase ITK is Critical for HIV-1 Infection of Jurkat T-cells.

Hain, Anika / Krämer, Melanie / Linka, René M / Nakhaei-Rad, Saeideh / Ahmadian, Mohammad Reza / Häussinger, Dieter / Borkhardt, Arndt / Münk, Carsten

Scientific reports

2018 Volume 8, Issue 1, Page(s) 3217

Abstract: Successful replication of Human immunodeficiency virus (HIV)-1 depends on the expression of various cellular host factors, such as the interleukin-2 inducible T-cell kinase (ITK), a member of the protein family of TEC-tyrosine kinases. ITK is selectively ...

Abstract	Successful replication of Human immunodeficiency virus (HIV)-1 depends on the expression of various cellular host factors, such as the interleukin-2 inducible T-cell kinase (ITK), a member of the protein family of TEC-tyrosine kinases. ITK is selectively expressed in T-cells and coordinates signaling pathways downstream of the T-cell receptor and chemokine receptors, including PLC-1 activation, Ca
MeSH term(s)	HIV/physiology ; HIV Infections/etiology ; Humans ; Interleukin-2/metabolism ; Jurkat Cells ; Protein-Tyrosine Kinases/deficiency ; Protein-Tyrosine Kinases/physiology ; Virus Internalization ; Virus Replication
Chemical Substances	IL2 protein, human ; Interleukin-2 ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; emt protein-tyrosine kinase (EC 2.7.10.2)
Language	English
Publishing date	2018-02-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-21344-7
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Article ; Online: The long non-coding RNA HOTAIRM1 promotes tumor aggressiveness and radiotherapy resistance in glioblastoma.

Ahmadov, Ulvi / Picard, Daniel / Bartl, Jasmin / Silginer, Manuela / Trajkovic-Arsic, Marija / Qin, Nan / Blümel, Lena / Wolter, Marietta / Lim, Jonathan K M / Pauck, David / Winkelkotte, Alina Marie / Melcher, Marlen / Langini, Maike / Marquardt, Viktoria / Sander, Felix / Stefanski, Anja / Steltgens, Sascha / Hassiepen, Christina / Kaufhold, Anna /

Meyer, Frauke-Dorothee / Seibt, Annette / Kleinesudeik, Lara / Hain, Anika / Münk, Carsten / Knobbe-Thomsen, Christiane Brigitte / Schramm, Alexander / Fischer, Ute / Leprivier, Gabriel / Stühler, Kai / Fulda, Simone / Siveke, Jens T / Distelmaier, Felix / Borkhardt, Arndt / Weller, Michael / Roth, Patrick / Reifenberger, Guido / Remke, Marc

Cell death & disease

2021 Volume 12, Issue 10, Page(s) 885

Abstract: Glioblastoma is the most common malignant primary brain tumor. To date, clinically relevant biomarkers are restricted to isocitrate dehydrogenase (IDH) gene 1 or 2 mutations and O6-methylguanine DNA methyltransferase (MGMT) promoter methylation. Long non- ...

Abstract	Glioblastoma is the most common malignant primary brain tumor. To date, clinically relevant biomarkers are restricted to isocitrate dehydrogenase (IDH) gene 1 or 2 mutations and O6-methylguanine DNA methyltransferase (MGMT) promoter methylation. Long non-coding RNAs (lncRNAs) have been shown to contribute to glioblastoma pathogenesis and could potentially serve as novel biomarkers. The clinical significance of HOXA Transcript Antisense RNA, Myeloid-Specific 1 (HOTAIRM1) was determined by analyzing HOTAIRM1 in multiple glioblastoma gene expression data sets for associations with prognosis, as well as, IDH mutation and MGMT promoter methylation status. Finally, the role of HOTAIRM1 in glioblastoma biology and radiotherapy resistance was characterized in vitro and in vivo. We identified HOTAIRM1 as a candidate lncRNA whose up-regulation is significantly associated with shorter survival of glioblastoma patients, independent from IDH mutation and MGMT promoter methylation. Glioblastoma cell line models uniformly showed reduced cell viability, decreased invasive growth and diminished colony formation capacity upon HOTAIRM1 down-regulation. Integrated proteogenomic analyses revealed impaired mitochondrial function and determination of reactive oxygen species (ROS) levels confirmed increased ROS levels upon HOTAIRM1 knock-down. HOTAIRM1 knock-down decreased expression of transglutaminase 2 (TGM2), a candidate protein implicated in mitochondrial function, and knock-down of TGM2 mimicked the phenotype of HOTAIRM1 down-regulation in glioblastoma cells. Moreover, HOTAIRM1 modulates radiosensitivity of glioblastoma cells both in vitro and in vivo. Our data support a role for HOTAIRM1 as a driver of biological aggressiveness, radioresistance and poor outcome in glioblastoma. Targeting HOTAIRM1 may be a promising new therapeutic approach.
MeSH term(s)	Animals ; Carcinogenesis/genetics ; Carcinogenesis/pathology ; Cell Line, Tumor ; Cell Survival/genetics ; Clone Cells ; Down-Regulation/genetics ; Gene Expression Regulation, Neoplastic ; Glioblastoma/genetics ; Glioblastoma/pathology ; Glioblastoma/radiotherapy ; Humans ; Mice, Nude ; MicroRNAs/genetics ; MicroRNAs/metabolism ; Mitochondria/metabolism ; Neoplasm Invasiveness ; Phenotype ; Prognosis ; Protein Glutamine gamma Glutamyltransferase 2/metabolism ; Proteogenomics ; RNA, Small Interfering/metabolism ; Radiation Tolerance/genetics ; Reactive Oxygen Species/metabolism ; Mice
Chemical Substances	MIRN17 microRNA, human ; MicroRNAs ; RNA, Small Interfering ; Reactive Oxygen Species ; long non-coding RNA HOTAIRM1, human ; Protein Glutamine gamma Glutamyltransferase 2 (EC 2.3.2.13)
Language	English
Publishing date	2021-09-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-021-04146-0
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Article ; Online: APOBEC4 Enhances the Replication of HIV-1.

Marino, Daniela / Perković, Mario / Hain, Anika / Jaguva Vasudevan, Ananda A / Hofmann, Henning / Hanschmann, Kay-Martin / Mühlebach, Michael D / Schumann, Gerald G / König, Renate / Cichutek, Klaus / Häussinger, Dieter / Münk, Carsten

PloS one

2016 Volume 11, Issue 6, Page(s) e0155422

Abstract: APOBEC4 (A4) is a member of the AID/APOBEC family of cytidine deaminases. In this study we found a high mRNA expression of A4 in human testis. In contrast, there were only low levels of A4 mRNA detectable in 293T, HeLa, Jurkat or A3.01 cells. Ectopic ... ...

Abstract	APOBEC4 (A4) is a member of the AID/APOBEC family of cytidine deaminases. In this study we found a high mRNA expression of A4 in human testis. In contrast, there were only low levels of A4 mRNA detectable in 293T, HeLa, Jurkat or A3.01 cells. Ectopic expression of A4 in HeLa cells resulted in mostly cytoplasmic localization of the protein. To test whether A4 has antiviral activity similar to that of proteins of the APOBEC3 (A3) subfamily, A4 was co-expressed in 293T cells with wild type HIV-1 and HIV-1 luciferase reporter viruses. We found that A4 did not inhibit the replication of HIV-1 but instead enhanced the production of HIV-1 in a dose-dependent manner and seemed to act on the viral LTR. A4 did not show detectable cytidine deamination activity in vitro and weakly interacted with single-stranded DNA. The presence of A4 in virus producer cells enhanced HIV-1 replication by transiently transfected A4 or stably expressed A4 in HIV-susceptible cells. APOBEC4 was capable of similarly enhancing transcription from a broad spectrum of promoters, regardless of whether they were viral or mammalian. We hypothesize that A4 may have a natural role in modulating host promoters or endogenous LTR promoters.
MeSH term(s)	Cell Line ; Cytidine/metabolism ; Cytidine Deaminase/metabolism ; Cytidine Deaminase/physiology ; Deamination ; HIV Long Terminal Repeat ; HIV-1/physiology ; Humans ; Male ; Promoter Regions, Genetic ; Testis/metabolism ; Virus Replication/physiology
Chemical Substances	Cytidine (5CSZ8459RP) ; APOBEC4 protein, human (EC 3.5.4.5) ; Cytidine Deaminase (EC 3.5.4.5)
Language	English
Publishing date	2016-06-01
Publishing country	United States
Document type	Journal Article
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0155422
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Article ; Online: Determinants of FIV and HIV Vif sensitivity of feline APOBEC3 restriction factors.

Zhang, Zeli / Gu, Qinyong / Jaguva Vasudevan, Ananda Ayyappan / Hain, Anika / Kloke, Björn-Philipp / Hasheminasab, Sascha / Mulnaes, Daniel / Sato, Kei / Cichutek, Klaus / Häussinger, Dieter / Bravo, Ignacio G / Smits, Sander H J / Gohlke, Holger / Münk, Carsten

Retrovirology

2016 Volume 13, Issue 1, Page(s) 46

Abstract: Background: Feline immunodeficiency virus (FIV) is a global pathogen of Felidae species and a model system for Human immunodeficiency virus (HIV)-induced AIDS. In felids such as the domestic cat (Felis catus), APOBEC3 (A3) genes encode for single-domain ...

Abstract	Background: Feline immunodeficiency virus (FIV) is a global pathogen of Felidae species and a model system for Human immunodeficiency virus (HIV)-induced AIDS. In felids such as the domestic cat (Felis catus), APOBEC3 (A3) genes encode for single-domain A3Z2s, A3Z3 and double-domain A3Z2Z3 anti-viral cytidine deaminases. The feline A3Z2Z3 is expressed following read-through transcription and alternative splicing, introducing a previously untranslated exon in frame, encoding a domain insertion called linker. Only A3Z3 and A3Z2Z3 inhibit Vif-deficient FIV. Feline A3s also are restriction factors for HIV and Simian immunodeficiency viruses (SIV). Surprisingly, HIV-2/SIV Vifs can counteract feline A3Z2Z3. Results: To identify residues in feline A3s that Vifs need for interaction and degradation, chimeric human-feline A3s were tested. Here we describe the molecular direct interaction of feline A3s with Vif proteins from cat FIV and present the first structural A3 model locating these interaction regions. In the Z3 domain we have identified residues involved in binding of FIV Vif, and their mutation blocked Vif-induced A3Z3 degradation. We further identified additional essential residues for FIV Vif interaction in the A3Z2 domain, allowing the generation of FIV Vif resistant A3Z2Z3. Mutated feline A3s also showed resistance to the Vif of a lion-specific FIV, indicating an evolutionary conserved Vif-A3 binding. Comparative modelling of feline A3Z2Z3 suggests that the residues interacting with FIV Vif have, unlike Vif-interacting residues in human A3s, a unique location at the domain interface of Z2 and Z3 and that the linker forms a homeobox-like domain protruding of the Z2Z3 core. HIV-2/SIV Vifs efficiently degrade feline A3Z2Z3 by possible targeting the linker stretch connecting both Z-domains. Conclusions: Here we identified in feline A3s residues important for binding of FIV Vif and a unique protein domain insertion (linker). To understand Vif evolution, a structural model of the feline A3 was developed. Our results show that HIV Vif binds human A3s differently than FIV Vif feline A3s. The linker insertion is suggested to form a homeo-box domain, which is unique to A3s of cats and related species, and not found in human and mouse A3s. Together, these findings indicate a specific and different A3 evolution in cats and human.
MeSH term(s)	Animals ; Cats ; Cell Line ; Cytidine Deaminase/chemistry ; Cytidine Deaminase/genetics ; Cytidine Deaminase/metabolism ; Evolution, Molecular ; Gene Products, vif/genetics ; Gene Products, vif/metabolism ; Genes, Homeobox ; HIV-1/genetics ; HIV-1/metabolism ; Humans ; Immunodeficiency Virus, Feline/genetics ; Immunodeficiency Virus, Feline/metabolism ; Models, Molecular ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Gene Products, vif ; Recombinant Fusion Proteins ; Cytidine Deaminase (EC 3.5.4.5)
Language	English
Publishing date	2016-07-01
Publishing country	England
Document type	Journal Article
ISSN	1742-4690
ISSN (online)	1742-4690
DOI	10.1186/s12977-016-0274-9
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Article ; Online: Iron regulation through the back door: iron-dependent metabolite levels contribute to transcriptional adaptation to iron deprivation in Saccharomyces cerevisiae.

Ihrig, Jessica / Hausmann, Anja / Hain, Anika / Richter, Nadine / Hamza, Iqbal / Lill, Roland / Mühlenhoff, Ulrich

Eukaryotic cell

2009 Volume 9, Issue 3, Page(s) 460–471

Abstract: Budding yeast (Saccharomyces cerevisiae) responds to iron deprivation both by Aft1-Aft2-dependent transcriptional activation of genes involved in cellular iron uptake and by Cth1-Cth2-specific degradation of certain mRNAs coding for iron-dependent ... ...

Abstract	Budding yeast (Saccharomyces cerevisiae) responds to iron deprivation both by Aft1-Aft2-dependent transcriptional activation of genes involved in cellular iron uptake and by Cth1-Cth2-specific degradation of certain mRNAs coding for iron-dependent biosynthetic components. Here, we provide evidence for a novel principle of iron-responsive gene expression. This regulatory mechanism is based on the modulation of transcription through the iron-dependent variation of levels of regulatory metabolites. As an example, the LEU1 gene of branched-chain amino acid biosynthesis is downregulated under iron-limiting conditions through depletion of the metabolic intermediate alpha-isopropylmalate, which functions as a key transcriptional coactivator of the Leu3 transcription factor. Synthesis of alpha-isopropylmalate involves the iron-sulfur protein Ilv3, which is inactivated under iron deficiency. As another example, decreased mRNA levels of the cytochrome c-encoding CYC1 gene under iron-limiting conditions involve heme-dependent transcriptional regulation via the Hap1 transcription factor. Synthesis of the iron-containing heme is directly correlated with iron availability. Thus, the iron-responsive expression of genes that are downregulated under iron-limiting conditions is conferred by two independent regulatory mechanisms: transcriptional regulation through iron-responsive metabolites and posttranscriptional mRNA degradation. Only the combination of the two processes provides a quantitative description of the response to iron deprivation in yeast.
MeSH term(s)	3-Isopropylmalate Dehydrogenase/genetics ; CCAAT-Binding Factor/genetics ; Ceruloplasmin/genetics ; Cytochromes c/genetics ; Cytochromes c/metabolism ; DNA-Binding Proteins/genetics ; Down-Regulation/genetics ; Ferrochelatase/metabolism ; Gene Expression/drug effects ; Gene Expression/genetics ; Gene Expression Regulation, Fungal/physiology ; Heme/metabolism ; Homeostasis/physiology ; Hydro-Lyases/genetics ; Hydro-Lyases/metabolism ; Iron/deficiency ; Iron/metabolism ; Iron Chelating Agents/pharmacology ; Isomerases/genetics ; Isomerases/metabolism ; Malates/metabolism ; Malates/pharmacology ; Peroxidases/genetics ; Phenanthrolines/pharmacology ; Promoter Regions, Genetic/genetics ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Terminator Regions, Genetic/genetics ; Trans-Activators/genetics ; Transcription Factors/genetics ; Tristetraprolin/genetics ; Up-Regulation/genetics
Chemical Substances	AFT1 protein, S cerevisiae ; CCAAT-Binding Factor ; CTH1 protein, S cerevisiae ; CYC1 protein, S cerevisiae ; DNA-Binding Proteins ; HAP1 protein, S cerevisiae ; HAP4 protein, S cerevisiae ; Iron Chelating Agents ; LEU3 protein, S cerevisiae ; Malates ; Phenanthrolines ; Saccharomyces cerevisiae Proteins ; TIS11 protein, S cerevisiae ; Trans-Activators ; Transcription Factors ; Tristetraprolin ; alpha-isopropylmalate (3237-44-3) ; Heme (42VZT0U6YR) ; bathophenanthroline (4A2B091F0G) ; Cytochromes c (9007-43-6) ; Iron (E1UOL152H7) ; 3-Isopropylmalate Dehydrogenase (EC 1.1.1.85) ; LEU2 protein, S cerevisiae (EC 1.1.1.85) ; HMX1 protein, S cerevisiae (EC 1.11.1.-) ; Peroxidases (EC 1.11.1.-) ; Ceruloplasmin (EC 1.16.3.1) ; FET3 protein, S cerevisiae (EC 1.16.3.1) ; Hydro-Lyases (EC 4.2.1.-) ; isopropylmalate isomerase (EC 4.2.1.33) ; dihydroxyacid dehydratase (EC 4.2.1.9) ; Ferrochelatase (EC 4.99.1.1) ; Isomerases (EC 5.-)
Language	English
Publishing date	2009-12-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2077635-4
ISSN	1535-9786 ; 1535-9778
ISSN (online)	1535-9786
ISSN	1535-9778
DOI	10.1128/EC.00213-09
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Article ; Online: Interferon but not MxB inhibits foamy retroviruses.

Bähr, Ariane / Singer, Anna / Hain, Anika / Vasudevan, Ananda Ayyappan Jaguva / Schilling, Mirjam / Reh, Juliane / Riess, Maximilian / Panitz, Sylvia / Serrano, Vanessa / Schweizer, Matthias / König, Renate / Chanda, Sumit / Häussinger, Dieter / Kochs, Georg / Lindemann, Dirk / Münk, Carsten

Virology

2016 Volume 488, Page(s) 51–60

Abstract: Foamy viruses (FV) are retroviruses that are widely distributed in primate and non-primate animal species. We tested here FV with capsids of simian and non-simian origin for sensitivity to interferon-β (IFN-β). Our data show significant inhibition of FV ... ...

Abstract	Foamy viruses (FV) are retroviruses that are widely distributed in primate and non-primate animal species. We tested here FV with capsids of simian and non-simian origin for sensitivity to interferon-β (IFN-β). Our data show significant inhibition of FV by IFN-β early in infection of human HOS and THP-1 but not of HEK293T cells. The post-entry restriction of FV was not mediated by the interferon-induced MxB protein that was recently identified as a capsid-interacting restriction factor targeting Human immunodeficiency virus (HIV) before integration. Neither the ectopic expression of MxA or MxB in HEK293T cells nor the lack of MxB expression in CRISPR/CAS MxB THP-1 knockout cells impacted the infection of the tested FV. IFN-β treated THP-1 and THP-1 KO MxB cells showed the same extend of restriction to FV. Together, the data demonstrate that IFN-β inhibits FV early in infection and that MxB is not a restriction factor of FV.
MeSH term(s)	Cell Line ; Humans ; Interferon-beta/metabolism ; Myxovirus Resistance Proteins/deficiency ; Myxovirus Resistance Proteins/metabolism ; Spumavirus/immunology
Chemical Substances	MX2 protein, human ; Myxovirus Resistance Proteins ; Interferon-beta (77238-31-4)
Language	English
Publishing date	2016-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2015.10.034
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Article ; Online: Biophysical Characterization of Nucleophosmin Interactions with Human Immunodeficiency Virus Rev and Herpes Simplex Virus US11.

Nouri, Kazem / Moll, Jens M / Milroy, Lech-Gustav / Hain, Anika / Dvorsky, Radovan / Amin, Ehsan / Lenders, Michael / Nagel-Steger, Luitgard / Howe, Sebastian / Smits, Sander H J / Hengel, Hartmut / Schmitt, Lutz / Münk, Carsten / Brunsveld, Luc / Ahmadian, Mohammad R

PloS one

2015 Volume 10, Issue 12, Page(s) e0143634

Abstract: Nucleophosmin (NPM1, also known as B23, numatrin or NO38) is a pentameric RNA-binding protein with RNA and protein chaperon functions. NPM1 has increasingly emerged as a potential cellular factor that directly associates with viral proteins; however, the ...

Abstract	Nucleophosmin (NPM1, also known as B23, numatrin or NO38) is a pentameric RNA-binding protein with RNA and protein chaperon functions. NPM1 has increasingly emerged as a potential cellular factor that directly associates with viral proteins; however, the significance of these interactions in each case is still not clear. In this study, we have investigated the physical interaction of NPM1 with both human immunodeficiency virus type 1 (HIV-1) Rev and Herpes Simplex virus type 1 (HSV-1) US11, two functionally homologous proteins. Both viral proteins show, in mechanistically different modes, high affinity for a binding site on the N-terminal oligomerization domain of NPM1. Rev, additionally, exhibits low-affinity for the central histone-binding domain of NPM1. We also showed that the proapoptotic cyclic peptide CIGB-300 specifically binds to NPM1 oligomerization domain and blocks its association with Rev and US11. Moreover, HIV-1 virus production was significantly reduced in the cells treated with CIGB-300. Results of this study suggest that targeting NPM1 may represent a useful approach for antiviral intervention.
MeSH term(s)	Animals ; Biophysical Phenomena ; COS Cells ; Chlorocebus aethiops ; HIV-1 ; HeLa Cells ; Humans ; Models, Molecular ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Peptides, Cyclic/metabolism ; Protein Binding ; Protein Multimerization ; Protein Structure, Quaternary ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Viral Proteins/chemistry ; Viral Proteins/metabolism ; rev Gene Products, Human Immunodeficiency Virus/chemistry ; rev Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	Nuclear Proteins ; Peptides, Cyclic ; RNA-Binding Proteins ; US11 protein, herpesvirus ; Viral Proteins ; rev Gene Products, Human Immunodeficiency Virus ; rev protein, Human Immunodeficiency Virus-1 ; nucleophosmin (117896-08-9) ; CIGB-300 (X6HMT2EDH9)
Language	English
Publishing date	2015-12-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0143634
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Article ; Online: APOBEC4 Enhances the Replication of HIV-1

Marino, Daniela / Perković, Mario / Hain, Anika / Vasudevan, Ananda A. Jaguva / Hofmann, Henning / Hanschmann, Kay-Martin / Mühlebach, Michael D. / Schumann, Gerald G. / König, Renate / Cichutek, Klaus / Häussinger, Dieter / Münk, Carsten

2016

Abstract	APOBEC4 (A4) is a member of the AID/APOBEC family of cytidine deaminases. In this study we found a high mRNA expression of A4 in human testis. In contrast, there were only low levels of A4 mRNA detectable in 293T, HeLa, Jurkat or A3.01 cells. Ectopic expression of A4 in HeLa cells resulted in mostly cytoplasmic localization of the protein. To test whether A4 has antiviral activity similar to that of proteins of the APOBEC3 (A3) subfamily, A4 was co-expressed in 293T cells with wild type HIV-1 and HIV-1 luciferase reporter viruses. We found that A4 did not inhibit the replication of HIV-1 but instead enhanced the production of HIV-1 in a dose-dependent manner and seemed to act on the viral LTR. A4 did not show detectable cytidine deamination activity in vitro and weakly interacted with single-stranded DNA. The presence of A4 in virus producer cells enhanced HIV-1 replication by transiently transfected A4 or stably expressed A4 in HIV-susceptible cells. APOBEC4 was capable of similarly enhancing transcription from a broad spectrum of promoters, regardless of whether they were viral or mammalian. We hypothesize that A4 may have a natural role in modulating host promoters or endogenous LTR promoters.
Keywords	Medizin ; ddc:610
Subject code	570
Language	English
Publishing date	2016-06-01
Publisher	Infektionskrankheiten / Erreger
Publishing country	de
Document type	Article ; Online
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Article ; Online: APOBEC4 Enhances the Replication of HIV-1

2016

Abstract	APOBEC4 (A4) is a member of the AID/APOBEC family of cytidine deaminases. In this study we found a high mRNA expression of A4 in human testis. In contrast, there were only low levels of A4 mRNA detectable in 293T, HeLa, Jurkat or A3.01 cells. Ectopic expression of A4 in HeLa cells resulted in mostly cytoplasmic localization of the protein. To test whether A4 has antiviral activity similar to that of proteins of the APOBEC3 (A3) subfamily, A4 was co-expressed in 293T cells with wild type HIV-1 and HIV-1 luciferase reporter viruses. We found that A4 did not inhibit the replication of HIV-1 but instead enhanced the production of HIV-1 in a dose-dependent manner and seemed to act on the viral LTR. A4 did not show detectable cytidine deamination activity in vitro and weakly interacted with single-stranded DNA. The presence of A4 in virus producer cells enhanced HIV-1 replication by transiently transfected A4 or stably expressed A4 in HIV-susceptible cells. APOBEC4 was capable of similarly enhancing transcription from a broad spectrum of promoters, regardless of whether they were viral or mammalian. We hypothesize that A4 may have a natural role in modulating host promoters or endogenous LTR promoters.
Keywords	610 Medizin ; ddc:610
Subject code	570
Language	English
Publishing date	2016-06-01
Publisher	Robert Koch-Institut, Infektionskrankheiten / Erreger
Publishing country	de
Document type	Article ; Online
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