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  1. Article ; Online: HIV-1 transmission: modelling and direct visualization in the third dimension.

    Coomer, Charles A / Padilla-Parra, Sergi

    Microscopy (Oxford, England)

    2023  Volume 72, Issue 3, Page(s) 164–177

    Abstract: Identifying initial events of mucosal entry of human immunodeficiency virus type-1 (HIV-1) in laboratory-based, physiologically relevant and high-throughput contexts may aid in designing effective strategies to block local transmission and spread of HIV- ... ...

    Abstract Identifying initial events of mucosal entry of human immunodeficiency virus type-1 (HIV-1) in laboratory-based, physiologically relevant and high-throughput contexts may aid in designing effective strategies to block local transmission and spread of HIV-1. Several paradigms have been posited for how HIV-1 crosses mucosal barriers to establish infection based on two dimensional (2D) culture-based or animal-based models. Nevertheless, despite these models stemming from 2D culture and animal studies, monolayers of cells poorly replicate the complex niche that influences viral entry at mucosal surfaces, whereas animal models often inadequately reproduce human disease pathophysiology and are prohibitively expensive. Organoids, having never been directly utilized in HIV-1 transmission investigations, may offer a compromise between 2D culture and animal models as they provide a platform that mimics the biophysical and biochemical niche of mucosal tissues. Importantly, observation of events downstream of viral inoculation is potentially accessible to researchers via an array of microscopy techniques. Because of the potential insights organoids may provide in this context, we offer this review to highlight key physiological factors of HIV-1 transmission at common mucosal sites and a discussion to highlight how many of these factors can be recapitulated in organoids, their current limitations and what questions can initially be addressed, particularly using a selective inclusion of quantitative light microscopy techniques. Harnessing organoids for direct observation of HIV-1 entry at mucosal sites may uncover potential therapeutic targets which prevent the establishment of HIV-1 infection.
    MeSH term(s) Animals ; Humans ; HIV-1/physiology ; HIV Infections/prevention & control ; Mucous Membrane ; Microscopy
    Language English
    Publishing date 2023-01-23
    Publishing country England
    Document type Review ; Journal Article
    ZDB-ID 2707496-1
    ISSN 2050-5701 ; 2050-5698
    ISSN (online) 2050-5701
    ISSN 2050-5698
    DOI 10.1093/jmicro/dfad014
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  2. Article: CD225 Proteins: A Family Portrait of Fusion Regulators.

    Coomer, Charles A / Rahman, Kazi / Compton, Alex A

    Trends in genetics : TIG

    2021  Volume 37, Issue 5, Page(s) 406–410

    Abstract: The CD225 superfamily regulates vesicular membrane fusion events essential to neurotransmission, immunity, development, and metabolism. Its importance to physiology is reinforced by the identification of polymorphisms associated with disease. This ... ...

    Abstract The CD225 superfamily regulates vesicular membrane fusion events essential to neurotransmission, immunity, development, and metabolism. Its importance to physiology is reinforced by the identification of polymorphisms associated with disease. This article highlights the shared features that drive the function of CD225 proteins such as interferon-inducible transmembrane proteins 3 (IFITM3) and proline-rich transmembrane protein 2 (PRRT2) and is intended to catalyze efforts towards characterizing the lesser-known family members.
    MeSH term(s) Animals ; Antigens, Differentiation/chemistry ; Antigens, Differentiation/genetics ; Antigens, Differentiation/metabolism ; Exocytosis/physiology ; Host-Pathogen Interactions/immunology ; Humans ; Membrane Fusion/physiology ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Membrane Proteins/metabolism ; Multigene Family ; Nerve Tissue Proteins/metabolism ; Virus Internalization
    Chemical Substances Antigens, Differentiation ; Membrane Proteins ; Nerve Tissue Proteins ; PRRT2 protein, human ; fragilis protein, mouse ; leu-13 antigen
    Language English
    Publishing date 2021-01-29
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 619240-3
    ISSN 1362-4555 ; 0168-9525 ; 0168-9479
    ISSN (online) 1362-4555
    ISSN 0168-9525 ; 0168-9479
    DOI 10.1016/j.tig.2021.01.004
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  3. Article ; Online: Correction: Single-cell glycolytic activity regulates membrane tension and HIV-1 fusion.

    Coomer, Charles A / Carlon-Andres, Irene / Iliopoulou, Maro / Dustin, Michael L / Compeer, Ewoud B / Compton, Alex A / Padilla-Parra, Sergi

    PLoS pathogens

    2021  Volume 17, Issue 5, Page(s) e1009584

    Abstract: This corrects the article DOI: 10.1371/journal.ppat.1008359.]. ...

    Abstract [This corrects the article DOI: 10.1371/journal.ppat.1008359.].
    Language English
    Publishing date 2021-05-10
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1009584
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  4. Article ; Online: Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state.

    Rahman, Kazi / Coomer, Charles A / Majdoul, Saliha / Ding, Selena Y / Padilla-Parra, Sergi / Compton, Alex A

    eLife

    2020  Volume 9

    Abstract: The interferon-inducible transmembrane (IFITM) proteins belong to the Dispanin/CD225 family and inhibit diverse virus infections. IFITM3 reduces membrane fusion between cells and virions through a poorly characterized mechanism. Mutation of proline-rich ... ...

    Abstract The interferon-inducible transmembrane (IFITM) proteins belong to the Dispanin/CD225 family and inhibit diverse virus infections. IFITM3 reduces membrane fusion between cells and virions through a poorly characterized mechanism. Mutation of proline-rich transmembrane protein 2 (PRRT2), a regulator of neurotransmitter release, at glycine-305 was previously linked to paroxysmal neurological disorders in humans. Here, we show that glycine-305 and the homologous site in IFITM3, glycine-95, drive protein oligomerization from within a GxxxG motif. Mutation of glycine-95 (and to a lesser extent, glycine-91) disrupted IFITM3 oligomerization and reduced its antiviral activity against Influenza A virus. An oligomerization-defective variant was used to reveal that IFITM3 promotes membrane rigidity in a glycine-95-dependent and amphipathic helix-dependent manner. Furthermore, a compound which counteracts virus inhibition by IFITM3, Amphotericin B, prevented the IFITM3-mediated rigidification of membranes. Overall, these data suggest that IFITM3 oligomers inhibit virus-cell fusion by promoting membrane rigidity.
    MeSH term(s) Amino Acid Motifs ; Cell Line ; HEK293 Cells ; Humans ; Influenza A virus/genetics ; Influenza A virus/physiology ; Influenza, Human/genetics ; Influenza, Human/immunology ; Influenza, Human/virology ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/immunology ; Virus Internalization
    Chemical Substances IFITM3 protein, human ; Membrane Proteins ; RNA-Binding Proteins
    Keywords covid19
    Language English
    Publishing date 2020-10-28
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.58537
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  5. Article ; Online: Single-cell glycolytic activity regulates membrane tension and HIV-1 fusion.

    Coomer, Charles A / Carlon-Andres, Irene / Iliopoulou, Maro / Dustin, Michael L / Compeer, Ewoud B / Compton, Alex A / Padilla-Parra, Sergi

    PLoS pathogens

    2020  Volume 16, Issue 2, Page(s) e1008359

    Abstract: There has been resurgence in determining the role of host metabolism in viral infection yet deciphering how the metabolic state of single cells affects viral entry and fusion remains unknown. Here, we have developed a novel assay multiplexing genetically- ...

    Abstract There has been resurgence in determining the role of host metabolism in viral infection yet deciphering how the metabolic state of single cells affects viral entry and fusion remains unknown. Here, we have developed a novel assay multiplexing genetically-encoded biosensors with single virus tracking (SVT) to evaluate the influence of global metabolic processes on the success rate of virus entry in single cells. We found that cells with a lower ATP:ADP ratio prior to virus addition were less permissive to virus fusion and infection. These results indicated a relationship between host metabolic state and the likelihood for virus-cell fusion to occur. SVT revealed that HIV-1 virions were arrested at hemifusion in glycolytically-inactive cells. Interestingly, cells acutely treated with glycolysis inhibitor 2-deoxyglucose (2-DG) become resistant to virus infection and also display less surface membrane cholesterol. Addition of cholesterol in these in glycolytically-inactive cells rescued the virus entry block at hemifusion and enabled completion of HIV-1 fusion. Further investigation with FRET-based membrane tension and membrane order reporters revealed a link between host cell glycolytic activity and host membrane order and tension. Indeed, cells treated with 2-DG possessed lower plasma membrane lipid order and higher tension values, respectively. Our novel imaging approach that combines lifetime imaging (FLIM) and SVT revealed not only changes in plasma membrane tension at the point of viral fusion, but also that HIV is less likely to enter cells at areas of higher membrane tension. We therefore have identified a connection between host cell glycolytic activity and membrane tension that influences HIV-1 fusion in real-time at the single-virus fusion level in live cells.
    MeSH term(s) CD4-Positive T-Lymphocytes ; Cell Fusion ; Cell Membrane/metabolism ; Glycolysis/physiology ; HIV-1/metabolism ; HIV-1/physiology ; Humans ; Membrane Fusion/genetics ; Membrane Fusion/physiology ; Primary Cell Culture ; Single-Cell Analysis ; Viral Envelope Proteins/metabolism ; Virion/metabolism ; Virus Internalization
    Chemical Substances Viral Envelope Proteins
    Language English
    Publishing date 2020-02-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1008359
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  6. Article ; Online: Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state

    Rahman, Kazi / Coomer, Charles A. / Majdoul, Saliha / Ding, Selena / Padilla-Parra, Sergi / Compton, Alex A.

    bioRxiv

    Abstract: The interferon-inducible transmembrane (IFITM) proteins belong to the Dispanin/CD225 family and inhibit diverse virus infections. IFITM3 reduces membrane fusion between cells and virions through a poorly characterized mechanism. We identified a GxxxG ... ...

    Abstract The interferon-inducible transmembrane (IFITM) proteins belong to the Dispanin/CD225 family and inhibit diverse virus infections. IFITM3 reduces membrane fusion between cells and virions through a poorly characterized mechanism. We identified a GxxxG motif in many CD225 proteins, including IFITM3 and proline rich transmembrane protein 2 (PRRT2). Mutation of PRRT2, a regulator of neurotransmitter release, at glycine-305 was previously linked to paroxysmal neurological disorders in humans. Here, we show that glycine-305 and the homologous site in IFITM3, glycine-95, drive protein oligomerization from within a GxxxG motif. Mutation of glycine-95 in IFITM3 disrupted its oligomerization and reduced its antiviral activity against Influenza A and HIV-1. The oligomerization-defective variant was used to reveal that IFITM3 promotes membrane rigidity in a glycine-95-dependent manner. Furthermore, a compound which counteracts virus inhibition by IFITM3, amphotericin B, prevented the IFITM3-mediated rigidification of membranes. Overall, these data suggest that IFITM3 oligomers inhibit virus-cell fusion by promoting membrane rigidity.
    Keywords covid19
    Publisher BioRxiv
    Document type Article ; Online
    DOI 10.1101/2020.05.14.096891
    Database COVID19

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  7. Article ; Online: Author Correction: A dynamic three-step mechanism drives the HIV-1 pre-fusion reaction.

    Iliopoulou, Maro / Nolan, Rory / Alvarez, Luis / Watanabe, Yasunori / Coomer, Charles A / Jakobsdottir, G Maria / Bowden, Thomas A / Padilla-Parra, Sergi

    Nature structural & molecular biology

    2019  Volume 26, Issue 6, Page(s) 526

    Abstract: In the version of this article initially published, the label above the top right plot in Fig. 3b (HXB2-Alexa Fluor 488) was incorrect. The correct label is 'HXB2-Alexa Fluor 405'. The error has been corrected in the HTML and PDF versions of the article. ...

    Abstract In the version of this article initially published, the label above the top right plot in Fig. 3b (HXB2-Alexa Fluor 488) was incorrect. The correct label is 'HXB2-Alexa Fluor 405'. The error has been corrected in the HTML and PDF versions of the article.
    Language English
    Publishing date 2019-04-26
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-019-0244-8
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  8. Article ; Online: A dynamic three-step mechanism drives the HIV-1 pre-fusion reaction.

    Iliopoulou, Maro / Nolan, Rory / Alvarez, Luis / Watanabe, Yasunori / Coomer, Charles A / Jakobsdottir, G Maria / Bowden, Thomas A / Padilla-Parra, Sergi

    Nature structural & molecular biology

    2018  Volume 25, Issue 9, Page(s) 814–822

    Abstract: Little is known about the intermolecular dynamics and stoichiometry of the interactions of the human immunodeficiency virus type 1 (HIV-1) envelope (Env) protein with its receptors and co-receptors on the host cell surface. Here we analyze time-resolved ... ...

    Abstract Little is known about the intermolecular dynamics and stoichiometry of the interactions of the human immunodeficiency virus type 1 (HIV-1) envelope (Env) protein with its receptors and co-receptors on the host cell surface. Here we analyze time-resolved HIV-1 Env interactions with T-cell surface glycoprotein CD4 (CD4) and C-C chemokine receptor type 5 (CCR5) or C-X-C chemokine receptor type 4 (CXCR4) on the surface of cells, by combining multicolor super-resolution localization microscopy (direct stochastic optical reconstruction microscopy) with fluorescence fluctuation spectroscopy imaging. Utilizing the primary isolate JR-FL and laboratory HXB2 strains, we reveal the time-resolved stoichiometry of CD4 and CCR5 or CXCR4 in the pre-fusion complex with HIV-1 Env. The HIV-1 Env pre-fusion dynamics for both R5- and X4-tropic strains consists of a three-step mechanism, which seems to differ in stoichiometry. Analyses with the monoclonal HIV-1-neutralizing antibody b12 indicate that the mechanism of inhibition differs between JR-FL and HXB2 Env. The molecular insights obtained here identify assemblies of HIV-1 Env with receptors and co-receptors as potential novel targets for inhibitor design.
    MeSH term(s) Animals ; CD4 Antigens/metabolism ; COS Cells ; Chlorocebus aethiops ; HEK293 Cells ; HIV-1/metabolism ; Humans ; Membrane Fusion ; Microscopy/methods ; Receptors, CCR5/metabolism ; Receptors, CXCR4/metabolism ; Spectrometry, Fluorescence/methods ; Viral Envelope Proteins/metabolism
    Chemical Substances CCR5 protein, human ; CD4 Antigens ; CXCR4 protein, human ; Receptors, CCR5 ; Receptors, CXCR4 ; Viral Envelope Proteins
    Language English
    Publishing date 2018-08-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-018-0113-x
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