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  1. Article ; Online: Characterization of a glycan-binding complex of minor pilins completes the analysis of

    Shahin, Meriam / Sheppard, Devon / Raynaud, Claire / Berry, Jamie-Lee / Gurung, Ishwori / Silva, Lisete M / Feizi, Ten / Liu, Yan / Pelicic, Vladimir

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 3, Page(s) e2216237120

    Abstract: Type 4 filaments (T4F)-of which type 4 pili (T4P) are the archetype-are a superfamily of nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin, which also contain minor pilins whose roles are often poorly understood. Here, we ...

    Abstract Type 4 filaments (T4F)-of which type 4 pili (T4P) are the archetype-are a superfamily of nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin, which also contain minor pilins whose roles are often poorly understood. Here, we complete the structure/function analysis of the full set of T4P pilins in the opportunistic bacterial pathogen
    MeSH term(s) Humans ; Fimbriae Proteins/genetics ; Fimbriae Proteins/chemistry ; Streptococcus sanguis ; Fimbriae, Bacterial/metabolism
    Chemical Substances Fimbriae Proteins (147680-16-8)
    Language English
    Publishing date 2023-01-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2216237120
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: 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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  2. Article ; Online: Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.

    Anger, Robin / Pieulle, Laetitia / Shahin, Meriam / Valette, Odile / Le Guenno, Hugo / Kosta, Artemis / Pelicic, Vladimir / Fronzes, Rémi

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 7143

    Abstract: Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy ( ... ...

    Abstract Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy (cryo-EM) led to structures of several T4F, revealing that the long N-terminal α-helix (α1) - the trademark of pilins - packs in the centre of the filaments to form a hydrophobic core. In diderm bacteria - all available bacterial T4F structures are from diderm species - a portion of α1 is melted (unfolded). Here we report that this architecture is conserved in phylogenetically distant monoderm species by determining the structure of Streptococcus sanguinis T4P. Our 3.7 Å resolution cryo-EM structure of S. sanguinis heteropolymeric T4P and the resulting full atomic model including all minor pilins highlight universal features of bacterial T4F and have widespread implications in understanding T4F biology.
    MeSH term(s) Fimbriae Proteins/chemistry ; Cryoelectron Microscopy/methods ; Fimbriae, Bacterial/chemistry ; Bacteria ; Polymers
    Chemical Substances Fimbriae Proteins (147680-16-8) ; Polymers
    Language English
    Publishing date 2023-11-06
    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/s41467-023-42872-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The Salmonella transmembrane effector SteD hijacks AP1-mediated vesicular trafficking for delivery to antigen-loading MHCII compartments.

    Godlee, Camilla / Cerny, Ondrej / Liu, Mei / Blundell, Samkeliso / Gallagher, Alanna E / Shahin, Meriam / Holden, David W

    PLoS pathogens

    2022  Volume 18, Issue 5, Page(s) e1010252

    Abstract: SteD is a transmembrane effector of the Salmonella SPI-2 type III secretion system that inhibits T cell activation by reducing the amounts of at least three proteins -major histocompatibility complex II (MHCII), CD86 and CD97 -from the surface of antigen- ...

    Abstract SteD is a transmembrane effector of the Salmonella SPI-2 type III secretion system that inhibits T cell activation by reducing the amounts of at least three proteins -major histocompatibility complex II (MHCII), CD86 and CD97 -from the surface of antigen-presenting cells. SteD specifically localises at the trans-Golgi network (TGN) and MHCII compartments; however, the targeting, membrane integration and trafficking of SteD are not understood. Using systematic mutagenesis, we identify distinct regions of SteD that are required for these processes. We show that SteD integrates into membranes of the ER/Golgi through a two-step mechanism of membrane recruitment from the cytoplasm followed by integration. SteD then migrates to and accumulates within the TGN. From here it hijacks the host adaptor protein (AP)1-mediated trafficking pathway from the TGN to MHCII compartments. AP1 binding and post-TGN trafficking require a short sequence in the N-terminal cytoplasmic tail of SteD that resembles the AP1-interacting dileucine sorting signal, but in inverted orientation, suggesting convergent evolution.
    MeSH term(s) Major Histocompatibility Complex ; Protein Transport ; Salmonella/metabolism ; Type III Secretion Systems/metabolism ; trans-Golgi Network/metabolism
    Chemical Substances Type III Secretion Systems
    Language English
    Publishing date 2022-05-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1010252
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Structural Basis of Teneurin-Latrophilin Interaction in Repulsive Guidance of Migrating Neurons.

    Del Toro, Daniel / Carrasquero-Ordaz, Maria A / Chu, Amy / Ruff, Tobias / Shahin, Meriam / Jackson, Verity A / Chavent, Matthieu / Berbeira-Santana, Miguel / Seyit-Bremer, Goenuel / Brignani, Sara / Kaufmann, Rainer / Lowe, Edward / Klein, Rüdiger / Seiradake, Elena

    Cell

    2020  Volume 180, Issue 2, Page(s) 323–339.e19

    Abstract: Teneurins are ancient metazoan cell adhesion receptors that control brain development and neuronal wiring in higher animals. The extracellular C terminus binds the adhesion GPCR Latrophilin, forming a trans-cellular complex with synaptogenic functions. ... ...

    Abstract Teneurins are ancient metazoan cell adhesion receptors that control brain development and neuronal wiring in higher animals. The extracellular C terminus binds the adhesion GPCR Latrophilin, forming a trans-cellular complex with synaptogenic functions. However, Teneurins, Latrophilins, and FLRT proteins are also expressed during murine cortical cell migration at earlier developmental stages. Here, we present crystal structures of Teneurin-Latrophilin complexes that reveal how the lectin and olfactomedin domains of Latrophilin bind across a spiraling beta-barrel domain of Teneurin, the YD shell. We couple structure-based protein engineering to biophysical analysis, cell migration assays, and in utero electroporation experiments to probe the importance of the interaction in cortical neuron migration. We show that binding of Latrophilins to Teneurins and FLRTs directs the migration of neurons using a contact repulsion-dependent mechanism. The effect is observed with cell bodies and small neurites rather than their processes. The results exemplify how a structure-encoded synaptogenic protein complex is also used for repulsive cell guidance.
    MeSH term(s) Animals ; Cell Adhesion/physiology ; Crystallography, X-Ray/methods ; HEK293 Cells ; Humans ; K562 Cells ; Membrane Glycoproteins/metabolism ; Membrane Glycoproteins/ultrastructure ; Membrane Proteins/metabolism ; Membrane Proteins/ultrastructure ; Mice ; Mice, Inbred C57BL/embryology ; Nerve Tissue Proteins/metabolism ; Nerve Tissue Proteins/ultrastructure ; Neurites/metabolism ; Neurogenesis/physiology ; Neurons/metabolism ; Platelet Glycoprotein GPIb-IX Complex/metabolism ; Platelet Glycoprotein GPIb-IX Complex/ultrastructure ; Protein Binding/physiology ; Proteins/metabolism ; Proteins/ultrastructure ; Receptors, Cell Surface/metabolism ; Receptors, Peptide/metabolism ; Receptors, Peptide/ultrastructure ; Synapses/metabolism ; Tenascin/metabolism ; Tenascin/ultrastructure
    Chemical Substances Membrane Glycoproteins ; Membrane Proteins ; Nerve Tissue Proteins ; Platelet Glycoprotein GPIb-IX Complex ; Proteins ; Receptors, Cell Surface ; Receptors, Peptide ; TENM2 protein, human ; TENM3 protein, human ; TENM4 protein, human ; Tenascin ; adhesion receptor ; alpha-latrotoxin receptor ; leucine-rich repeat proteins ; teneurin-1
    Language English
    Publishing date 2020-01-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2019.12.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1167: 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)
    Zs.MG 58: Show issues

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