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  1. Article ; Online: Draft Genome Sequences of Six Moroccan Helicobacter pylori Isolates Belonging to the hspWAfrica Group.

    Kartti, Souad / Bouihat, Najat / El Hajjami, Nargisse / Ouadghiri, Mouna / Aanniz, Tarik / Elouennass, Mostafa / Belyamani, Lahcen / Ibrahimi, Azeddine / Benaouda, Amina

    Microbiology resource announcements

    2020  Volume 9, Issue 41

    Abstract: Helicobacter ... ...

    Abstract Helicobacter pylori
    Language English
    Publishing date 2020-10-08
    Publishing country United States
    Document type Journal Article
    ISSN 2576-098X
    ISSN (online) 2576-098X
    DOI 10.1128/MRA.00714-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: The inner-rod component of Shigella flexneri type 3 secretion system, MxiI, is involved in the transmission of the secretion activation signal by its interaction with MxiC.

    El Hajjami, Nargisse / Moussa, Simon / Houssa, Jonathan / Monteyne, Daniel / Perez-Morga, David / Botteaux, Anne

    MicrobiologyOpen

    2017  Volume 7, Issue 1

    Abstract: The virulence of Shigella mainly resides in the use of a Type 3 Secretion System (T3SS) to inject several proteins inside the host cell. Three categories of proteins are hierarchically secreted: (1) the needle components (MxiH and MxiI), (2) the ... ...

    Abstract The virulence of Shigella mainly resides in the use of a Type 3 Secretion System (T3SS) to inject several proteins inside the host cell. Three categories of proteins are hierarchically secreted: (1) the needle components (MxiH and MxiI), (2) the translocator proteins which form a pore (translocon) inside the host cell membrane, and (3) the effectors interfering with the host cell signaling pathways. In the absence of host cell contact, the T3SS is maintained in an "off" state by the presence of a tip complex. We have previously identified a gatekeeper protein, MxiC, which sequesters effectors inside the bacteria probably by interacting with MxiI, the inner-rod component. Upon cell contact and translocon insertion, a signal is most likely transmitted from the top of the needle to the base, passing through the needle and allowing effectors release. However, the molecular mechanism underlying the transmission of the activation signal through the needle is still poorly understood. In this work, we investigate the role of MxiI in the activation of the T3SS by performing a mutational study. Interestingly we have shown that mutations of a single residue in MxiI (T82) induce an mxiC-like phenotype and prevent the interaction with MxiC. Moreover, we have shown that the L26A mutation significantly reduces T3 secretion. The L26A mutation impairs the interaction between MxiI and Spa40, a keystone component of the switch between needle assembly and translocators secretion. The L26A mutation also sequesters MxiC. All these results highlight the crucial role of MxiI in regulating the secretion and transmitting the activation signal of the T3SS.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; DNA Mutational Analysis ; Protein Interaction Mapping ; Shigella flexneri/genetics ; Shigella flexneri/metabolism ; Signal Transduction ; Type III Secretion Systems/genetics ; Type III Secretion Systems/metabolism
    Chemical Substances Bacterial Proteins ; MxiI protein, Shigella flexneri ; Type III Secretion Systems
    Language English
    Publishing date 2017-12-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661368-2
    ISSN 2045-8827 ; 2045-8827
    ISSN (online) 2045-8827
    ISSN 2045-8827
    DOI 10.1002/mbo3.520
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Draft Genome Sequence of Stenotrophomonas maltophilia MDMC339, Isolated from Soil of Merzouga Desert in Morocco.

    Chemao-Elfihri, M W / Manni, Amina / Laamarti, Meriem / Kartti, Souad / Essabbar, Abdelmounim / Alouane, Tarek / Temsamani, Loubna / Eljamali, Jamal-Eddine / Ouadghiri, Mouna / El Hajjami, Nargisse / Sbabou, Laila / Belyamani, Lahcen / Ibrahimi, Azeddine / Filali-Maltouf, Abdelkarim

    Microbiology resource announcements

    2020  Volume 9, Issue 32

    Abstract: Here, we report the draft genome sequence ... ...

    Abstract Here, we report the draft genome sequence of
    Language English
    Publishing date 2020-08-06
    Publishing country United States
    Document type Journal Article
    ISSN 2576-098X
    ISSN (online) 2576-098X
    DOI 10.1128/MRA.00634-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Escape of intracellular Shigella from autophagy requires binding to cholesterol through the type III effector, IcsB.

    Kayath, Christian Aimé / Hussey, Seamus / El hajjami, Nargisse / Nagra, Karan / Philpott, Dana / Allaoui, Abdelmounaaïm

    Microbes and infection

    2010  Volume 12, Issue 12-13, Page(s) 956–966

    Abstract: Type III secretion systems are present in many pathogenic bacteria and mediate the translocation of bacterial effectors into host cells. Identification of host targets of these effectors is crucial for understanding bacterial virulence. IcsB, a type III ... ...

    Abstract Type III secretion systems are present in many pathogenic bacteria and mediate the translocation of bacterial effectors into host cells. Identification of host targets of these effectors is crucial for understanding bacterial virulence. IcsB, a type III secretion effector, helps Shigella to evade the host autophagy defense system by binding to the autophagy protein, Atg5. Here, we show that IcsB is able to interact specifically with cholesterol. The cholesterol binding domain (CBD) of IcsB is located between residues 288 and 351. Specific mutations of single tyrosine residues Y297 or Y340 of IcsB by phenylalanine (F) slightly reduced cholesterol binding, whereas deletion of the entire CBD or double mutation Y297F-Y340F strongly abolished interactions with cholesterol. To determine whether Shigella expressing IcsB variants could evade autophagy as effectively as the wild-type Shigella, we infected MDAMC cells stably expressing the autophagy marker LC3 fused to GFP and bacterial autophagosome formation was quantified using fluorescence microscopy. Mutation Y297F or Y340F slightly impaired IcsB function, whereas complete removal of CBD or mutation Y297F-Y340F significantly impaired autophagy evasion. Furthermore, we report that BopA, the counterpart of IcsB in Burkholderia pseudomallei with similar autophagy-evading properties, contains the CBD domain and is also able to bind cholesterol.
    MeSH term(s) Autophagy ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Burkholderia pseudomallei/immunology ; Burkholderia pseudomallei/metabolism ; Cell Line ; Cholesterol/metabolism ; Host-Pathogen Interactions ; Humans ; Mutant Proteins/genetics ; Mutant Proteins/metabolism ; Mutation ; Protein Binding ; Sequence Deletion ; Shigella flexneri/immunology ; Shigella flexneri/metabolism ; Virulence Factors/genetics ; Virulence Factors/metabolism
    Chemical Substances Bacterial Proteins ; Mutant Proteins ; Virulence Factors ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2010-11
    Publishing country France
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1465093-9
    ISSN 1769-714X ; 1286-4579
    ISSN (online) 1769-714X
    ISSN 1286-4579
    DOI 10.1016/j.micinf.2010.06.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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