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  1. Article ; Online: A Proteomic Analysis of Detergent-Resistant Membranes in HIV Virological Synapse: The Involvement of Vimentin in CD4 Polarization.

    Iida, Naoyuki / Kawahara, Madoka / Hirota, Riku / Shibagaki, Yoshio / Hattori, Seisuke / Morikawa, Yuko

    Viruses

    2023  Volume 15, Issue 6

    Abstract: The cell-cell contact between HIV-1-infected and uninfected cells forms a virological synapse (VS) to allow for efficient HIV-1 transmission. Not only are HIV-1 components polarized and accumulate at cell-cell interfaces, but viral receptors and lipid ... ...

    Abstract The cell-cell contact between HIV-1-infected and uninfected cells forms a virological synapse (VS) to allow for efficient HIV-1 transmission. Not only are HIV-1 components polarized and accumulate at cell-cell interfaces, but viral receptors and lipid raft markers are also. To better understand the nature of the HIV-1 VS, detergent-resistant membrane (DRM) fractions were isolated from an infected-uninfected cell coculture and compared to those from non-coculture samples using 2D fluorescence difference gel electrophoresis. Mass spectrometry revealed that ATP-related enzymes (ATP synthase subunit and vacuolar-type proton ATPase), protein translation factors (eukaryotic initiation factor 4A and mitochondrial elongation factor Tu), protein quality-control-related factors (protein disulfide isomerase A3 and 26S protease regulatory subunit), charged multivesicular body protein 4B, and vimentin were recruited to the VS. Membrane flotation centrifugation of the DRM fractions and confocal microscopy confirmed these findings. We further explored how vimentin contributes to the HIV-1 VS and found that vimentin supports HIV-1 transmission through the recruitment of CD4 to the cell-cell interface. Since many of the molecules identified in this study have previously been suggested to be involved in HIV-1 infection, we suggest that a 2D difference gel analysis of DRM-associated proteins may reveal the molecules that play crucial roles in HIV-1 cell-cell transmission.
    MeSH term(s) Humans ; Detergents/pharmacology ; Vimentin/metabolism ; Proteomics/methods ; HIV Infections/metabolism ; Adenosine Triphosphate/metabolism ; Membrane Microdomains/metabolism
    Chemical Substances Detergents ; Vimentin ; Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2023-05-28
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v15061266
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: HIV Reactivation in Latently Infected Cells With Virological Synapse-Like Cell Contact.

    Okutomi, Toshiki / Minakawa, Satoko / Hirota, Riku / Katagiri, Koko / Morikawa, Yuko

    Viruses

    2020  Volume 12, Issue 4

    Abstract: HIV reactivation from latency is induced by cytokines but also by cell contact with other cells. To better understand this, J1.1 cells, a latent HIV-1-infected Jurkat derivative, were cocultured with its parental Jurkat. J1.1 cells became p17MA-positive ... ...

    Abstract HIV reactivation from latency is induced by cytokines but also by cell contact with other cells. To better understand this, J1.1 cells, a latent HIV-1-infected Jurkat derivative, were cocultured with its parental Jurkat. J1.1 cells became p17MA-positive and produced a high level of HIV p24CA antigen, only when they were cocultured with stimulated Jurkat with cell-to-cell contact. In contrast, very little p24CA was produced when they were cocultured without cell contact. Similar results were obtained when latent ACH-2 and its parental A3.01 cells were cocultured. Confocal microscopy revealed that not only HIV-1 p17MA and gp120Env but also LFA-1, CD81, CD59, and TCR CD3 accumulated at the cell contact site, suggesting formation of the virological synapse-like structure. LFA-1-ICAM-1 interaction was involved in the cell-to-cell contact. When J1.1 was cocultured with TCR-deficient Jurkat, the p17MA-positive rate was significantly lower, although the cell-to-cell contact was not impaired. Quantitative proteomics identified 54 membrane molecules, one of which was MHC class I, that accumulated at the cell contact site. Reactivation from latency was also influenced by the presence of stromal cells. Our study indicated that latent HIV-1 in J1.1/ACH-2 cells was efficiently reactivated by cell-to-cell contact with stimulated parental cells, accompanying the virological synapse-like structure.
    MeSH term(s) Cell Communication ; Coculture Techniques ; Fluorescent Antibody Technique ; HIV Infections/virology ; HIV-1/physiology ; Host-Pathogen Interactions ; Humans ; Intercellular Adhesion Molecule-1/metabolism ; Jurkat Cells ; Lymphocyte Activation/immunology ; Lymphocyte Function-Associated Antigen-1/metabolism ; Protein Binding ; Stromal Cells ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism ; Virus Activation ; Virus Latency
    Chemical Substances ICAM1 protein, human ; Lymphocyte Function-Associated Antigen-1 ; Intercellular Adhesion Molecule-1 (126547-89-5)
    Language English
    Publishing date 2020-04-08
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12040417
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: HIV Reactivation in Latently Infected Cells with Virological Synapse-Like Cell Contact

    Okutomi, Toshiki / Minakawa, Satoko / Hirota, Riku / Katagiri, Koko / Morikawa, Yuko

    Viruses. 2020 Apr. 08, v. 12, no. 4

    2020  

    Abstract: HIV reactivation from latency is induced by cytokines but also by cell contact with other cells. To better understand this, J1.1 cells, a latent HIV-1-infected Jurkat derivative, were cocultured with its parental Jurkat. J1.1 cells became p17MA-positive ... ...

    Abstract HIV reactivation from latency is induced by cytokines but also by cell contact with other cells. To better understand this, J1.1 cells, a latent HIV-1-infected Jurkat derivative, were cocultured with its parental Jurkat. J1.1 cells became p17MA-positive and produced a high level of HIV p24CA antigen, only when they were cocultured with stimulated Jurkat with cell-to-cell contact. In contrast, very little p24CA was produced when they were cocultured without cell contact. Similar results were obtained when latent ACH-2 and its parental A3.01 cells were cocultured. Confocal microscopy revealed that not only HIV-1 p17MA and gp120Env but also LFA-1, CD81, CD59, and TCR CD3 accumulated at the cell contact site, suggesting formation of the virological synapse-like structure. LFA-1–ICAM-1 interaction was involved in the cell-to-cell contact. When J1.1 was cocultured with TCR-deficient Jurkat, the p17MA-positive rate was significantly lower, although the cell-to-cell contact was not impaired. Quantitative proteomics identified 54 membrane molecules, one of which was MHC class I, that accumulated at the cell contact site. Reactivation from latency was also influenced by the presence of stromal cells. Our study indicated that latent HIV-1 in J1.1/ACH-2 cells was efficiently reactivated by cell-to-cell contact with stimulated parental cells, accompanying the virological synapse-like structure.
    Keywords HIV infections ; Human immunodeficiency virus 1 ; antigens ; coculture ; confocal microscopy ; cytokines ; major histocompatibility complex ; proteomics ; stromal cells
    Language English
    Dates of publication 2020-0408
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12040417
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Tat-exported peptidoglycan amidase-dependent cell division contributes to Salmonella Typhimurium fitness in the inflamed gut.

    Fujimoto, Mayuka / Goto, Ryosuke / Hirota, Riku / Ito, Masahiro / Haneda, Takeshi / Okada, Nobuhiko / Miki, Tsuyoshi

    PLoS pathogens

    2018  Volume 14, Issue 10, Page(s) e1007391

    Abstract: Salmonella enterica serovar Typhimurium (S. Tm) is a cause of food poisoning accompanied with gut inflammation. Although mucosal inflammation is generally thought to be protective against bacterial infection, S. Tm exploits the inflammation to compete ... ...

    Abstract Salmonella enterica serovar Typhimurium (S. Tm) is a cause of food poisoning accompanied with gut inflammation. Although mucosal inflammation is generally thought to be protective against bacterial infection, S. Tm exploits the inflammation to compete with commensal microbiota, thereby growing up to high densities in the gut lumen and colonizing the gut continuously at high levels. However, the molecular mechanisms underlying the beneficial effect of gut inflammation on S. Tm competitive growth are poorly understood. Notably, the twin-arginine translocation (Tat) system, which enables the transport of folded proteins outside bacterial cytoplasm, is well conserved among many bacterial pathogens, with Tat substrates including virulence factors and virulence-associated proteins. Here, we show that Tat and Tat-exported peptidoglycan amidase, AmiA- and AmiC-dependent cell division contributes to S. Tm competitive fitness advantage in the inflamed gut. S. Tm tatC or amiA amiC mutants feature a gut colonization defect, wherein they display a chain form of cells. The chains are attributable to a cell division defect of these mutants and occur in inflamed but not in normal gut. We demonstrate that attenuated resistance to bile acids confers the colonization defect on the S. Tm amiA amiC mutant. In particular, S. Tm cell chains are highly sensitive to bile acids as compared to single or paired cells. Furthermore, we show that growth media containing high concentrations of NaCl and sublethal concentrations of antimicrobial peptides induce the S. Tm amiA amiC mutant chain form, suggesting that gut luminal conditions such as high osmolarity and the presence of antimicrobial peptides impose AmiA- and AmiC-dependent cell division on S. Tm. Together, our data indicate that Tat and the Tat-exported amidases, AmiA and AmiC, are required for S. Tm luminal fitness in the inflamed gut, suggesting that these proteins might comprise effective targets for novel antibacterial agents against infectious diarrhea.
    MeSH term(s) Amidohydrolases/metabolism ; Animals ; Cell Division ; Gastrointestinal Tract/metabolism ; Gastrointestinal Tract/microbiology ; Gastrointestinal Tract/pathology ; Inflammation/metabolism ; Inflammation/microbiology ; Inflammation/pathology ; Mice ; Mice, Inbred C57BL ; Peptidoglycan/metabolism ; Salmonella Infections, Animal/metabolism ; Salmonella Infections, Animal/microbiology ; Salmonella Infections, Animal/pathology ; Salmonella typhimurium/physiology ; Twin-Arginine-Translocation System/metabolism
    Chemical Substances Peptidoglycan ; Twin-Arginine-Translocation System ; Amidohydrolases (EC 3.5.-) ; amidase (EC 3.5.1.4)
    Language English
    Publishing date 2018-10-31
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1007391
    Database MEDical Literature Analysis and Retrieval System OnLINE

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