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  1. Article ; Online: DDX41 Recognizes RNA/DNA Retroviral Reverse Transcripts and Is Critical for

    Stavrou, Spyridon / Aguilera, Alexya N / Blouch, Kristin / Ross, Susan R

    mBio

    2018  Volume 9, Issue 3

    Abstract: Host recognition of viral nucleic acids generated during infection leads to the activation of innate immune responses essential for early control of virus. Retrovirus reverse transcription creates numerous potential ligands for cytosolic host sensors ... ...

    Abstract Host recognition of viral nucleic acids generated during infection leads to the activation of innate immune responses essential for early control of virus. Retrovirus reverse transcription creates numerous potential ligands for cytosolic host sensors that recognize foreign nucleic acids, including single-stranded RNA (ssRNA), RNA/DNA hybrids, and double-stranded DNA (dsDNA). We and others recently showed that the sensors cyclic GMP-AMP synthase (cGAS), DEAD-box helicase 41 (DDX41), and members of the Aim2-like receptor (ALR) family participate in the recognition of retroviral reverse transcripts. However, why multiple sensors might be required and their relative importance in
    MeSH term(s) Animals ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; DNA, Viral/chemistry ; DNA, Viral/genetics ; DNA, Viral/metabolism ; Dendritic Cells/enzymology ; Dendritic Cells/virology ; Host-Pathogen Interactions ; Humans ; Leukemia Virus, Murine/genetics ; Leukemia Virus, Murine/physiology ; Macrophages/enzymology ; Macrophages/virology ; Male ; Mice ; Mice, Inbred C57BL ; Nucleotidyltransferases/genetics ; Nucleotidyltransferases/metabolism ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Retroviridae Infections/enzymology ; Retroviridae Infections/genetics ; Retroviridae Infections/virology
    Chemical Substances DNA, Viral ; RNA, Viral ; Nucleotidyltransferases (EC 2.7.7.-) ; cGAS protein, mouse (EC 2.7.7.-) ; DDX41 protein, mouse (EC 3.6.4.13) ; DEAD-box RNA Helicases (EC 3.6.4.13)
    Language English
    Publishing date 2018-06-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.00923-18
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Deaminase-Dead Mouse APOBEC3 Is an

    Stavrou, Spyridon / Zhao, Wenming / Blouch, Kristin / Ross, Susan R

    Journal of virology

    2018  Volume 92, Issue 11

    Abstract: The apolipoprotein B editing complex 3 (APOBEC3) proteins are potent retroviral restriction factors that are under strong positive selection, both in terms of gene copy number and sequence diversity. A common feature of all the members of the APOBEC3 ... ...

    Abstract The apolipoprotein B editing complex 3 (APOBEC3) proteins are potent retroviral restriction factors that are under strong positive selection, both in terms of gene copy number and sequence diversity. A common feature of all the members of the APOBEC3 family is the presence of one or two cytidine deamination domains, essential for cytidine deamination of retroviral reverse transcripts as well as packaging into virions. Several studies have indicated that human and mouse APOBEC3 proteins restrict retrovirus infection via cytidine deaminase (CD)-dependent and -independent means. To understand the relative contribution of CD-independent restriction
    MeSH term(s) Animals ; Cell Line ; Cytidine Deaminase/genetics ; Cytidine Deaminase/metabolism ; Deamination/genetics ; HEK293 Cells ; Humans ; Leukemia Virus, Murine/genetics ; Leukemia Virus, Murine/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; RNA, Viral/genetics ; RNA-Directed DNA Polymerase/genetics ; Retroviridae Infections/prevention & control ; Reverse Transcriptase Inhibitors/metabolism ; Reverse Transcription/genetics
    Chemical Substances RNA, Viral ; Reverse Transcriptase Inhibitors ; RNA-Directed DNA Polymerase (EC 2.7.7.49) ; Apobec3 protein, mouse (EC 3.5.4.5) ; Cytidine Deaminase (EC 3.5.4.5)
    Language English
    Publishing date 2018-05-14
    Publishing country United States
    Document type 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.00168-18
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  3. Article ; Online: In Vivo Examination of Mouse APOBEC3- and Human APOBEC3A- and APOBEC3G-Mediated Restriction of Parvovirus and Herpesvirus Infection in Mouse Models.

    Nakaya, Yuki / Stavrou, Spyridon / Blouch, Kristin / Tattersall, Peter / Ross, Susan R

    Journal of virology

    2016  Volume 90, Issue 17, Page(s) 8005–8012

    Abstract: Unlabelled: APOBEC3 knockout and human APOBEC3A and -3G transgenic mice were tested for their ability to be infected by the herpesviruses herpes simplex virus 1 and murine herpesvirus 68 and the parvovirus minute virus of mice (MVM). Knockout, APOBEC3A ... ...

    Abstract Unlabelled: APOBEC3 knockout and human APOBEC3A and -3G transgenic mice were tested for their ability to be infected by the herpesviruses herpes simplex virus 1 and murine herpesvirus 68 and the parvovirus minute virus of mice (MVM). Knockout, APOBEC3A and APOBEC3G transgenic, and wild-type mice were equally infected by the herpesviruses, while APOBEC3A but not mouse APOBEC3 conferred resistance to MVM. No viruses showed evidence of cytidine deamination by mouse or human APOBEC3s. These data suggest that in vitro studies implicating APOBEC3 proteins in virus resistance may not reflect their role in vivo
    Importance: It is well established that APOBEC3 proteins in different species are a critical component of the host antiretroviral defense. Whether these proteins also function to inhibit other viruses is not clear. There have been a number of in vitro studies suggesting that different APOBEC3 proteins restrict herpesviruses and parvoviruses, among others, but whether they also work in vivo has not been demonstrated. Our studies looking at the role of mouse and human APOBEC3 proteins in transgenic and knockout mouse models of viral infection suggest that these restriction factors are not broadly antiviral and demonstrate the importance of testing their activity in vivo.
    MeSH term(s) APOBEC-3G Deaminase/metabolism ; Animals ; Cytidine Deaminase/metabolism ; Disease Models, Animal ; Disease Resistance ; Herpesviridae Infections/immunology ; Herpesvirus 1, Human/immunology ; Mice ; Mice, Knockout ; Mice, Transgenic ; Minute Virus of Mice/immunology ; Parvoviridae Infections/immunology ; Proteins/metabolism ; Rhadinovirus/immunology
    Chemical Substances Proteins ; APOBEC-3G Deaminase (EC 3.5.4.5) ; APOBEC3A protein, human (EC 3.5.4.5) ; APOBEC3G protein, human (EC 3.5.4.5) ; Apobec3 protein, mouse (EC 3.5.4.5) ; Cytidine Deaminase (EC 3.5.4.5)
    Language English
    Publishing date 2016-09-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.00973-16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Nucleic acid recognition orchestrates the anti-viral response to retroviruses.

    Stavrou, Spyridon / Blouch, Kristin / Kotla, Swathi / Bass, Antonia / Ross, Susan R

    Cell host & microbe

    2015  Volume 17, Issue 4, Page(s) 478–488

    Abstract: Intrinsic restriction factors and viral nucleic acid sensors are important for the anti-viral response. Here, we show how upstream sensing of retroviral reverse transcripts integrates with the downstream effector APOBEC3, an IFN-induced cytidine ... ...

    Abstract Intrinsic restriction factors and viral nucleic acid sensors are important for the anti-viral response. Here, we show how upstream sensing of retroviral reverse transcripts integrates with the downstream effector APOBEC3, an IFN-induced cytidine deaminase that introduces lethal mutations during retroviral reverse transcription. Using a murine leukemia virus (MLV) variant with an unstable capsid that induces a strong IFNβ antiviral response, we identify three sensors, IFI203, DDX41, and cGAS, required for MLV nucleic acid recognition. These sensors then signal using the adaptor STING, leading to increased production of IFNβ and other targets downstream of the transcription factor IRF3. Using knockout and mutant mice, we show that APOBEC3 limits the levels of reverse transcripts that trigger cytosolic sensing, and that nucleic acid sensing in vivo increases expression of IFN-regulated restriction factors like APOBEC3 that in turn reduce viral load. These studies underscore the importance of the multiple layers of protection afforded by host factors.
    MeSH term(s) Animals ; Cell Line ; Cytidine Deaminase/metabolism ; DEAD-box RNA Helicases/metabolism ; DNA, Viral/metabolism ; Interferon-beta/metabolism ; Leukemia Virus, Murine/immunology ; Leukemia Virus, Murine/physiology ; Macrophages/immunology ; Macrophages/virology ; Membrane Proteins/metabolism ; Mice, Inbred C57BL ; Mice, Knockout ; Nuclear Proteins/metabolism ; Nucleotidyltransferases/metabolism ; Reverse Transcription ; Signal Transduction
    Chemical Substances DNA, Viral ; Ifi203 protein, mouse ; Membrane Proteins ; Nuclear Proteins ; Sting1 protein, mouse ; Interferon-beta (77238-31-4) ; Nucleotidyltransferases (EC 2.7.7.-) ; cGAS protein, mouse (EC 2.7.7.-) ; Apobec3 protein, mouse (EC 3.5.4.5) ; Cytidine Deaminase (EC 3.5.4.5) ; DDX41 protein, mouse (EC 3.6.4.13) ; DEAD-box RNA Helicases (EC 3.6.4.13)
    Language English
    Publishing date 2015-03-26
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2278004-X
    ISSN 1934-6069 ; 1931-3128
    ISSN (online) 1934-6069
    ISSN 1931-3128
    DOI 10.1016/j.chom.2015.02.021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6578: Show issues Location:
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  5. Article ; Online: Different modes of retrovirus restriction by human APOBEC3A and APOBEC3G in vivo.

    Stavrou, Spyridon / Crawford, Daniel / Blouch, Kristin / Browne, Edward P / Kohli, Rahul M / Ross, Susan R

    PLoS pathogens

    2014  Volume 10, Issue 5, Page(s) e1004145

    Abstract: The apolipoprotein B editing complex 3 (A3) cytidine deaminases are among the most highly evolutionarily selected retroviral restriction factors, both in terms of gene copy number and sequence diversity. Primate genomes encode seven A3 genes, and while ... ...

    Abstract The apolipoprotein B editing complex 3 (A3) cytidine deaminases are among the most highly evolutionarily selected retroviral restriction factors, both in terms of gene copy number and sequence diversity. Primate genomes encode seven A3 genes, and while A3F and 3G are widely recognized as important in the restriction of HIV, the role of the other genes, particularly A3A, is not as clear. Indeed, since human cells can express multiple A3 genes, and because of the lack of an experimentally tractable model, it is difficult to dissect the individual contribution of each gene to virus restriction in vivo. To overcome this problem, we generated human A3A and A3G transgenic mice on a mouse A3 knockout background. Using these mice, we demonstrate that both A3A and A3G restrict infection by murine retroviruses but by different mechanisms: A3G was packaged into virions and caused extensive deamination of the retrovirus genomes while A3A was not packaged and instead restricted infection when expressed in target cells. Additionally, we show that a murine leukemia virus engineered to express HIV Vif overcame the A3G-mediated restriction, thereby creating a novel model for studying the interaction between these proteins. We have thus developed an in vivo system for understanding how human A3 proteins use different modes of restriction, as well as a means for testing therapies that disrupt HIV Vif-A3G interactions.
    MeSH term(s) APOBEC-3G Deaminase ; Animals ; Cells, Cultured ; Cytidine Deaminase/physiology ; HIV-1/physiology ; Humans ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; NIH 3T3 Cells ; Proteins/physiology ; Retroviridae/physiology ; Retroviridae Infections/genetics ; Retroviridae Infections/virology ; Viral Load/genetics ; Virus Assembly/genetics ; Virus Internalization ; Virus Replication/genetics ; vif Gene Products, Human Immunodeficiency Virus/genetics
    Chemical Substances Proteins ; vif Gene Products, Human Immunodeficiency Virus ; vif protein, Human immunodeficiency virus 1 ; APOBEC-3G Deaminase (EC 3.5.4.5) ; APOBEC3A protein, human (EC 3.5.4.5) ; APOBEC3G protein, human (EC 3.5.4.5) ; Cytidine Deaminase (EC 3.5.4.5)
    Language English
    Publishing date 2014-05-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1004145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Human chimeric antigen receptor macrophages for cancer immunotherapy.

    Klichinsky, Michael / Ruella, Marco / Shestova, Olga / Lu, Xueqing Maggie / Best, Andrew / Zeeman, Martha / Schmierer, Maggie / Gabrusiewicz, Konrad / Anderson, Nicholas R / Petty, Nicholas E / Cummins, Katherine D / Shen, Feng / Shan, Xinhe / Veliz, Kimberly / Blouch, Kristin / Yashiro-Ohtani, Yumi / Kenderian, Saad S / Kim, Miriam Y / O'Connor, Roddy S /
    Wallace, Stephen R / Kozlowski, Miroslaw S / Marchione, Dylan M / Shestov, Maksim / Garcia, Benjamin A / June, Carl H / Gill, Saar

    Nature biotechnology

    2020  Volume 38, Issue 8, Page(s) 947–953

    Abstract: Chimeric antigen receptor (CAR) T cell therapy has shown promise in hematologic malignancies, but its application to solid tumors has been ... ...

    Abstract Chimeric antigen receptor (CAR) T cell therapy has shown promise in hematologic malignancies, but its application to solid tumors has been challenging
    MeSH term(s) Animals ; Cell Line, Tumor ; Cell Survival ; Humans ; Immunotherapy ; Immunotherapy, Adoptive ; Lung Neoplasms/therapy ; Macrophages/physiology ; Mice ; Microscopy, Video ; Neoplasms/therapy ; Neoplasms, Experimental
    Language English
    Publishing date 2020-03-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1311932-1
    ISSN 1546-1696 ; 1087-0156
    ISSN (online) 1546-1696
    ISSN 1087-0156
    DOI 10.1038/s41587-020-0462-y
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    Zs.A 2167: Show issues Location:
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  7. Article: Checkpoint Blockade Reverses Anergy in IL-13Rα2 Humanized scFv-Based CAR T Cells to Treat Murine and Canine Gliomas.

    Yin, Yibo / Boesteanu, Alina C / Binder, Zev A / Xu, Chong / Reid, Reiss A / Rodriguez, Jesse L / Cook, Danielle R / Thokala, Radhika / Blouch, Kristin / McGettigan-Croce, Bevin / Zhang, Logan / Konradt, Christoph / Cogdill, Alexandria P / Panjwani, M Kazim / Jiang, Shuguang / Migliorini, Denis / Dahmane, Nadia / Posey, Avery D / June, Carl H /
    Mason, Nicola J / Lin, Zhiguo / O'Rourke, Donald M / Johnson, Laura A

    Molecular therapy oncolytics

    2018  Volume 11, Page(s) 20–38

    Abstract: We generated two humanized interleukin-13 receptor α2 (IL-13Rα2) chimeric antigen receptors (CARs), Hu07BBz and Hu08BBz, that recognized human IL-13Rα2, but not IL-13Rα1. Hu08BBz also recognized canine IL-13Rα2. Both of these CAR T cell constructs ... ...

    Abstract We generated two humanized interleukin-13 receptor α2 (IL-13Rα2) chimeric antigen receptors (CARs), Hu07BBz and Hu08BBz, that recognized human IL-13Rα2, but not IL-13Rα1. Hu08BBz also recognized canine IL-13Rα2. Both of these CAR T cell constructs demonstrated superior tumor inhibitory effects in a subcutaneous xenograft model of human glioma compared with a humanized EGFRvIII CAR T construct used in a recent phase 1 clinical trial (ClinicalTrials.gov: NCT02209376). The Hu08BBz demonstrated a 75% reduction in orthotopic tumor growth using low-dose CAR T cell infusion. Using combination therapy with immune checkpoint blockade, humanized IL-13Rα2 CAR T cells performed significantly better when combined with CTLA-4 blockade, and humanized EGFRvIII CAR T cells' efficacy was improved by PD-1 and TIM-3 blockade in the same mouse model, which was correlated with the levels of checkpoint molecule expression in co-cultures with the same tumor
    Language English
    Publishing date 2018-08-28
    Publishing country United States
    Document type Journal Article
    ISSN 2372-7705
    ISSN 2372-7705
    DOI 10.1016/j.omto.2018.08.002
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