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  1. Article ; Online: Syntaxin 11 Contributes to the Interferon-Inducible Restriction of Coxiella burnetii Intracellular Infection.

    Ganesan, Sandhya / Alvarez, Natalie N / Steiner, Samuel / Fowler, Karen M / Corona, Abigail K / Roy, Craig R

    mBio

    2023  Volume 14, Issue 1, Page(s) e0354522

    Abstract: There is a limited understanding of host defense mechanisms targeting intracellular pathogens that proliferate in a lysosome. Coxiella burnetii is a model bacterial pathogen capable of replicating in the hydrolytic and acidic environment of the lysosome. ...

    Abstract There is a limited understanding of host defense mechanisms targeting intracellular pathogens that proliferate in a lysosome. Coxiella burnetii is a model bacterial pathogen capable of replicating in the hydrolytic and acidic environment of the lysosome. It has been shown that gamma interferon (IFNγ)-stimulated host cells restrict C. burnetii replication by a mechanism that involves host IDO1 depletion of tryptophan. Host cells deficient in IDO1 activity, however, retain the ability to restrict C. burnetii replication when stimulated with IFNγ, which suggests additional mechanisms of host defense. This study identified syntaxin 11 (STX11) as a host protein that contributes to IFNγ-mediated suppression of C. burnetii replication. STX11 is a SNARE protein; SNARE proteins are proteins that mediate fusion of host vesicles with specific subcellular organelles. Depletion of STX11 using either small interfering RNA (siRNA)- or CRISPR-based approaches enhanced C. burnetii replication intracellularly. Stable expression of STX11 reduced C. burnetii replication in epithelial cells and macrophages, which indicates that this STX11-dependent cell-autonomous response is operational in multiple cell types and can function independently of other IFNγ-induced factors. Fluorescently tagged STX11 localized to the
    MeSH term(s) Humans ; Coxiella burnetii ; Host-Pathogen Interactions/physiology ; Interferon-gamma/metabolism ; Interferons/metabolism ; Q Fever/metabolism ; Qa-SNARE Proteins/genetics ; Qa-SNARE Proteins/metabolism ; RNA, Small Interfering/metabolism ; Vacuoles/metabolism
    Chemical Substances Interferon-gamma (82115-62-6) ; Interferons (9008-11-1) ; Qa-SNARE Proteins ; RNA, Small Interfering ; STX11 protein, human
    Language English
    Publishing date 2023-02-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.03545-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Biochemical functions and structure of Caenorhabditis elegans ZK177.8 protein: Aicardi-Goutières syndrome SAMHD1 dNTPase ortholog.

    Maehigashi, Tatsuya / Lim, Christopher / Wade, Lydia R / Bowen, Nicole E / Knecht, Kirsten M / Alvarez, Natalie N / Kelly, William G / Schinazi, Raymond F / Kim, Dong-Hyun / Xiong, Yong / Kim, Baek

    The Journal of biological chemistry

    2023  Volume 299, Issue 9, Page(s) 105148

    Abstract: Mutations in sterile alpha motif domain and histidine-aspartate domain-containing protein 1 (SAMHD1) are found in a neurodevelopmental disorder, Aicardi-Goutières syndrome, and cancers, and SAMHD1, which is a deoxynucleoside triphosphate (dNTP) ... ...

    Abstract Mutations in sterile alpha motif domain and histidine-aspartate domain-containing protein 1 (SAMHD1) are found in a neurodevelopmental disorder, Aicardi-Goutières syndrome, and cancers, and SAMHD1, which is a deoxynucleoside triphosphate (dNTP) triphosphorylase, was identified as a myeloid-specific HIV-1 restriction factor. Here, we characterized the enzymology and structure of an SAMHD1 ortholog of Caenorhabditis elegans, ZK177.8, which also reportedly induces developmental defects upon gene knockdown. We found ZK177.8 protein is a dNTPase allosterically regulated by dGTP. The active site of ZK177.8 recognizes both 2' OH and triphosphate moieties of dNTPs but not base moiety. The dGTP activator induces the formation of the enzymatically active ZK177.8 tetramers, and ZK177.8 protein lowers cellular dNTP levels in a human monocytic cell line. Finally, ZK177.8 tetramers display very similar X-ray crystal structure with human and mouse SAMHD1s except that its lack of the canonical sterile alpha motif domain. This striking conservation in structure, function, and allosteric regulatory mechanism for the hydrolysis of the DNA building blocks supports their host developmental roles.
    Language English
    Publishing date 2023-08-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.105148
    Database MEDical Literature Analysis and Retrieval System OnLINE

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