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  1. Article ; Online: Editorial: Single cell analysis of bacteria-host interaction.

    Cerny, Ondrej / Godlee, Camilla / Lobato-Márquez, Damián

    Frontiers in cellular and infection microbiology

    2023  Volume 13, Page(s) 1196905

    MeSH term(s) Bacteria ; Host Microbial Interactions ; Single-Cell Analysis
    Language English
    Publishing date 2023-04-21
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2023.1196905
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  2. Article ; Online: Measuring Plasmid Stability in Gram-Negative Bacteria.

    Lobato-Márquez, Damián

    Methods in molecular biology (Clifton, N.J.)

    2019  Volume 2075, Page(s) 223–233

    Abstract: In this chapter, a highly sensitive method to measure plasmid stability in Gram-negative bacteria is described. This procedure is based on the counterselection of plasmid-containing cells using an aph-parE cassette. When bacteria carrying the aph-parE ... ...

    Abstract In this chapter, a highly sensitive method to measure plasmid stability in Gram-negative bacteria is described. This procedure is based on the counterselection of plasmid-containing cells using an aph-parE cassette. When bacteria carrying the aph-parE module in the plasmid of interest are grown in media containing rhamnose as the only carbon source, the P
    MeSH term(s) Genes, Bacterial ; Genetic Engineering ; Genomic Instability ; Gram-Negative Bacteria/genetics ; Plasmids/genetics ; Polymerase Chain Reaction
    Language English
    Publishing date 2019-10-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-9877-7_16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Regulation of integrin α5β1-mediated Staphylococcus aureus cellular invasion by the septin cytoskeleton.

    Robertin, Stevens / Brokatzky, Dominik / Lobato-Márquez, Damián / Mostowy, Serge

    European journal of cell biology

    2023  Volume 102, Issue 4, Page(s) 151359

    Abstract: Staphylococcus aureus, a Gram-positive bacterial pathogen, is an urgent health threat causing a wide range of clinical infections. Originally viewed as a strict extracellular pathogen, accumulating evidence has revealed S. aureus to be a facultative ... ...

    Abstract Staphylococcus aureus, a Gram-positive bacterial pathogen, is an urgent health threat causing a wide range of clinical infections. Originally viewed as a strict extracellular pathogen, accumulating evidence has revealed S. aureus to be a facultative intracellular pathogen subverting host cell signalling to support invasion. The majority of clinical isolates produce fibronectin-binding proteins A and B (FnBPA and FnBPB) to interact with host integrin α5β1, a key component of focal adhesions. S. aureus binding of integrin α5β1 promotes its clustering on the host cell surface, triggering activation of focal adhesion kinase (FAK) and cytoskeleton rearrangements to promote bacterial invasion into non-phagocytic cells. Here, we discover that septins, a component of the cytoskeleton that assembles on membranes, are recruited as collar-like structures with actin to S. aureus invasion sites engaging integrin α5β1. To investigate septin recruitment to the plasma membrane in a bacteria-free system, we used FnBPA-coated latex beads and showed that septins are recruited upon activation of integrin α5β1. SEPT2 depletion reduced S. aureus invasion, but increased surface expression of integrin α5 and adhesion of S. aureus to host cells. Consistent with this, SEPT2 depletion increased cellular protein levels of integrin α5 and β1 subunits, as well as FAK. Collectively, these results provide insights into regulation of integrin α5β1 and invasion of S. aureus by the septin cytoskeleton.
    MeSH term(s) Staphylococcus aureus/metabolism ; Integrin alpha5beta1/metabolism ; Septins/metabolism ; Integrin alpha5/metabolism ; Fibronectins ; Cytoskeleton/metabolism
    Chemical Substances Integrin alpha5beta1 ; Septins (EC 3.6.1.-) ; Integrin alpha5 ; Fibronectins
    Language English
    Publishing date 2023-09-03
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 391967-5
    ISSN 1618-1298 ; 0070-2463 ; 0171-9335
    ISSN (online) 1618-1298
    ISSN 0070-2463 ; 0171-9335
    DOI 10.1016/j.ejcb.2023.151359
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    Zs.A 667: Show issues Location:
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  4. Article ; Online: Septins and K63 ubiquitin chains are present in separate bacterial microdomains during autophagy of entrapped Shigella.

    Lobato-Márquez, Damián / Conesa, José Javier / López-Jiménez, Ana Teresa / Divine, Michael E / Pruneda, Jonathan N / Mostowy, Serge

    Journal of cell science

    2023  Volume 136, Issue 7

    Abstract: During host cell invasion, Shigella escapes to the cytosol and polymerizes actin for cell-to-cell spread. To restrict cell-to-cell spread, host cells employ cell-autonomous immune responses including antibacterial autophagy and septin cage entrapment. ... ...

    Abstract During host cell invasion, Shigella escapes to the cytosol and polymerizes actin for cell-to-cell spread. To restrict cell-to-cell spread, host cells employ cell-autonomous immune responses including antibacterial autophagy and septin cage entrapment. How septins interact with the autophagy process to target Shigella for destruction is poorly understood. Here, we employed a correlative light and cryo-soft X-ray tomography (cryo-SXT) pipeline to study Shigella septin cage entrapment in its near-native state. Quantitative cryo-SXT showed that Shigella fragments mitochondria and enabled visualization of X-ray-dense structures (∼30 nm resolution) surrounding Shigella entrapped in septin cages. Using Airyscan confocal microscopy, we observed lysine 63 (K63)-linked ubiquitin chains decorating septin-cage-entrapped Shigella. Remarkably, septins and K63 chains are present in separate bacterial microdomains, indicating they are recruited separately during antibacterial autophagy. Cryo-SXT and live-cell imaging revealed an interaction between septins and LC3B-positive membranes during autophagy of Shigella. Together, these findings demonstrate how septin-caged Shigella are targeted for autophagy and provide fundamental insights into autophagy-cytoskeleton interactions.
    MeSH term(s) Septins/metabolism ; Shigella/metabolism ; Cytoskeleton/metabolism ; Autophagy/physiology ; Ubiquitins/metabolism
    Chemical Substances Septins (EC 3.6.1.-) ; Ubiquitins
    Language English
    Publishing date 2023-04-13
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.261139
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1200: Show issues Location:
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  5. Article ; Online: Interplay between septins and ubiquitin-mediated xenophagy during

    Lobato-Márquez, Damián / Conesa, José Javier / López-Jiménez, Ana Teresa / Divine, Michael E / Pruneda, Jonathan N / Mostowy, Serge

    Autophagy reports

    2023  Volume 2, Issue 1

    Abstract: Septins are cytoskeletal proteins implicated in numerous cellular processes including cytokinesis and morphogenesis. In the case of infection ... ...

    Abstract Septins are cytoskeletal proteins implicated in numerous cellular processes including cytokinesis and morphogenesis. In the case of infection by
    Language English
    Publishing date 2023-05-17
    Publishing country United States
    Document type Journal Article
    ISSN 2769-4127
    ISSN (online) 2769-4127
    DOI 10.1080/27694127.2023.2213541
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  6. Article ; Online: Salmonella

    Lobato-Márquez, Damián / Mostowy, Serge

    EMBO reports

    2017  Volume 18, Issue 9, Page(s) 1476–1477

    MeSH term(s) Carrier Proteins/genetics ; Humans ; Salmonella ; Ubiquitin-Protein Ligases/genetics ; Ubiquitination
    Chemical Substances Carrier Proteins ; ARIH1 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2017-08-18
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.201744672
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    Zs.A 5433: Show issues Location:
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  7. Article ; Online: Septins recognize micron-scale membrane curvature.

    Lobato-Márquez, Damián / Mostowy, Serge

    The Journal of cell biology

    2016  Volume 213, Issue 1, Page(s) 5–6

    Abstract: How cells recognize membrane curvature is not fully understood. In this issue, Bridges et al. (2016.J. Cell Biol.http://dx.doi.org/10.1083/jcb.201512029) discover that septins, a component of the cytoskeleton, recognize membrane curvature at the micron ... ...

    Abstract How cells recognize membrane curvature is not fully understood. In this issue, Bridges et al. (2016.J. Cell Biol.http://dx.doi.org/10.1083/jcb.201512029) discover that septins, a component of the cytoskeleton, recognize membrane curvature at the micron scale, a common morphological hallmark of eukaryotic cellular processes.
    MeSH term(s) Humans ; Septins
    Chemical Substances Septins (EC 3.6.1.-)
    Language English
    Publishing date 2016-04-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201603063
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  8. Article ; Online: Mechanistic insight into bacterial entrapment by septin cage reconstitution.

    Lobato-Márquez, Damián / Xu, Jingwei / Güler, Gizem Özbaykal / Ojiakor, Adaobi / Pilhofer, Martin / Mostowy, Serge

    Nature communications

    2021  Volume 12, Issue 1, Page(s) 4511

    Abstract: Septins are cytoskeletal proteins that assemble into hetero-oligomeric complexes and sense micron-scale membrane curvature. During infection with Shigella flexneri, an invasive enteropathogen, septins restrict actin tail formation by entrapping bacteria ... ...

    Abstract Septins are cytoskeletal proteins that assemble into hetero-oligomeric complexes and sense micron-scale membrane curvature. During infection with Shigella flexneri, an invasive enteropathogen, septins restrict actin tail formation by entrapping bacteria in cage-like structures. Here, we reconstitute septin cages in vitro using purified recombinant septin complexes (SEPT2-SEPT6-SEPT7), and study how these recognize bacterial cells and assemble on their surface. We show that septin complexes recognize the pole of growing Shigella cells. An amphipathic helix domain in human SEPT6 enables septins to sense positively curved membranes and entrap bacterial cells. Shigella strains lacking lipopolysaccharide components are more efficiently entrapped in septin cages. Finally, cryo-electron tomography of in vitro cages reveals how septins assemble as filaments on the bacterial cell surface.
    MeSH term(s) Actins/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Membrane/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Dysentery, Bacillary/metabolism ; Dysentery, Bacillary/microbiology ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HeLa Cells ; Humans ; Lipopolysaccharides/metabolism ; Microscopy, Fluorescence ; Mutation ; Protein Binding ; Recombinant Proteins/metabolism ; Septins/genetics ; Septins/metabolism ; Shigella flexneri/genetics ; Shigella flexneri/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances Actins ; Bacterial Proteins ; DNA-Binding Proteins ; Lipopolysaccharides ; Recombinant Proteins ; Transcription Factors ; virG protein, Shigella flexneri ; Green Fluorescent Proteins (147336-22-9) ; SEPTIN6 protein, human (EC 3.6.1.-) ; Septins (EC 3.6.1.-)
    Language English
    Publishing date 2021-07-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-021-24721-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Septins promote caspase activity and coordinate mitochondrial apoptosis.

    Van Ngo, Hoan / Robertin, Stevens / Brokatzky, Dominik / Bielecka, Magdalena K / Lobato-Márquez, Damián / Torraca, Vincenzo / Mostowy, Serge

    Cytoskeleton (Hoboken, N.J.)

    2022  Volume 80, Issue 7-8, Page(s) 254–265

    Abstract: Apoptosis is a form of regulated cell death essential for tissue homeostasis and embryonic development. Apoptosis also plays a key role during bacterial infection, yet some intracellular bacterial pathogens (such as Shigella flexneri, whose ... ...

    Abstract Apoptosis is a form of regulated cell death essential for tissue homeostasis and embryonic development. Apoptosis also plays a key role during bacterial infection, yet some intracellular bacterial pathogens (such as Shigella flexneri, whose lipopolysaccharide can block apoptosis) can manipulate cell death programs as an important survival strategy. Septins are a component of the cytoskeleton essential for mitochondrial dynamics and host defense, however, the role of septins in regulated cell death is mostly unknown. Here, we discover that septins promote mitochondrial (i.e., intrinsic) apoptosis in response to treatment with staurosporine (a pan-kinase inhibitor) or etoposide (a DNA topoisomerase inhibitor). Consistent with a role for septins in mitochondrial dynamics, septins promote the release of mitochondrial protein cytochrome c in apoptotic cells and are required for the proteolytic activation of caspase-3, caspase-7, and caspase-9 (core components of the apoptotic machinery). Apoptosis of HeLa cells induced in response to infection by S. flexneri ΔgalU (a lipopolysaccharide mutant unable to block apoptosis) is also septin-dependent. In vivo, zebrafish larvae are significantly more susceptible to infection with S. flexneri ΔgalU (as compared to infection with wildtype S. flexneri), yet septin deficient larvae are equally susceptible to infection with S. flexneri ΔgalU and wildtype S. flexneri. These data provide a new molecular framework to understand the complexity of mitochondrial apoptosis and its ability to combat bacterial infection.
    Language English
    Publishing date 2022-05-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2534372-5
    ISSN 1949-3592 ; 1949-3584
    ISSN (online) 1949-3592
    ISSN 1949-3584
    DOI 10.1002/cm.21696
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    Zs.A 1840: Show issues Location:
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  10. Article ; Online: Acquisition of a large virulence plasmid (pINV) promoted temperature-dependent virulence and global dispersal of O96:H19 enteroinvasive

    Miles, Sydney L / Torraca, Vincenzo / Dyson, Zoe A / López-Jiménez, Ana Teresa / Foster-Nyarko, Ebenezer / Lobato-Márquez, Damián / Jenkins, Claire / Holt, Kathryn E / Mostowy, Serge

    mBio

    2023  Volume 14, Issue 4, Page(s) e0088223

    Abstract: ... ...

    Abstract Enteroinvasive
    MeSH term(s) Animals ; Humans ; Escherichia coli ; Virulence/genetics ; Zebrafish ; Dysentery, Bacillary ; Type III Secretion Systems/genetics ; Bayes Theorem ; Temperature ; Plasmids/genetics ; Shigella/genetics ; Escherichia coli Infections
    Chemical Substances Type III Secretion Systems
    Language English
    Publishing date 2023-05-31
    Publishing country United States
    Document type Journal Article ; 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.00882-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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