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  1. Article ; Online: P2RX7 at the Host-Pathogen Interface of Infectious Diseases.

    Soare, Alexandra Y / Freeman, Tracey L / Min, Alice K / Malik, Hagerah S / Osota, Elizabeth O / Swartz, Talia H

    Microbiology and molecular biology reviews : MMBR

    2021  Volume 85, Issue 1

    Abstract: The P2X7 receptor (P2RX7) is an important molecule that functions as a danger sensor, detecting extracellular nucleotides from injured cells and thus signaling an inflammatory program to nearby cells. It is expressed in immune cells and plays important ... ...

    Abstract The P2X7 receptor (P2RX7) is an important molecule that functions as a danger sensor, detecting extracellular nucleotides from injured cells and thus signaling an inflammatory program to nearby cells. It is expressed in immune cells and plays important roles in pathogen surveillance and cell-mediated responses to infectious organisms. There is an abundance of literature on the role of P2RX7 in inflammatory diseases and the role of these receptors in host-pathogen interactions. Here, we describe the current knowledge of the role of P2RX7 in the host response to a variety of pathogens, including viruses, bacteria, fungi, protozoa, and helminths. We describe
    MeSH term(s) Alarmins/immunology ; Animals ; Bacteria/immunology ; Fungi/immunology ; Helminths/immunology ; Host-Pathogen Interactions/immunology ; Host-Pathogen Interactions/physiology ; Humans ; Inflammation/immunology ; Parasites/immunology ; Receptors, Purinergic P2X7/immunology ; Signal Transduction/immunology ; Viruses/immunology
    Chemical Substances Alarmins ; P2RX7 protein, human ; Receptors, Purinergic P2X7
    Language English
    Publishing date 2021-01-13
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1376131-6
    ISSN 1098-5557 ; 1070-6275 ; 1092-2172
    ISSN (online) 1098-5557 ; 1070-6275
    ISSN 1092-2172
    DOI 10.1128/MMBR.00055-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.96: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: P2X1 Selective Antagonists Block HIV-1 Infection through Inhibition of Envelope Conformation-Dependent Fusion.

    Soare, Alexandra Y / Malik, Hagerah S / Durham, Natasha D / Freeman, Tracey L / Alvarez, Raymond / Patel, Foramben / Satija, Namita / Upadhyay, Chitra / Hioe, Catarina E / Chen, Benjamin K / Swartz, Talia H

    Journal of virology

    2020  Volume 94, Issue 6

    Abstract: Purinergic receptors are well-established modulators of inflammatory processes, primarily through detection of extracellular nucleotides that are released by dying or infected cells. Emerging literature has demonstrated that inhibition of these ... ...

    Abstract Purinergic receptors are well-established modulators of inflammatory processes, primarily through detection of extracellular nucleotides that are released by dying or infected cells. Emerging literature has demonstrated that inhibition of these inflammatory receptors can block HIV-1 productive infection and HIV-1-associated inflammation. The specificity of receptor type and mechanism of interaction has not yet been determined. Here, we characterize the inhibitory activity of P2X1 receptor antagonists, NF279 and NF449, in cell lines, primary cells, and a variety of HIV-1 envelope (Env) clades. NF279 and NF449 blocked productive infection at the level of viral membrane fusion, with a range of inhibitory activities against different HIV-1 Env isolates. A mutant virus carrying a truncation deletion of the C-terminal tail of HIV-1 Env glycoprotein 41 (gp41) showed reduced sensitivity to P2X1 antagonists, indicating that the sensitivity of inhibition by these molecules may be modulated by Env conformation. In contrast, a P2X7 antagonist, A438079, had a limited effect on productive infection and fusion. NF279 and NF449 interfered with the ability of the gp120 variable regions 1 and 2 (V1V2)-targeted broadly neutralizing antibody PG9 to block productive infection, suggesting that these drugs may antagonize HIV-1 Env at gp120 V1V2 to block viral membrane fusion. Our observations indicate that P2X1 antagonism can inhibit HIV-1 replication at the level of viral membrane fusion through interaction with Env. Future studies will probe the nature of these compounds in inhibiting HIV-1 fusion and the development of small molecules to block HIV-1 entry via this mechanism.
    MeSH term(s) HIV Envelope Protein gp120/genetics ; HIV Envelope Protein gp120/metabolism ; HIV Infections/drug therapy ; HIV Infections/genetics ; HIV Infections/metabolism ; HIV Infections/pathology ; HIV-1/genetics ; HIV-1/metabolism ; Humans ; Mutation ; Purinergic P2X Receptor Antagonists/pharmacology ; Virus Internalization/drug effects
    Chemical Substances HIV Envelope Protein gp120 ; Purinergic P2X Receptor Antagonists
    Language English
    Publishing date 2020-02-28
    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.01622-19
    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)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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