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  1. Article ; Online: Detergents with Scalable Properties Identify Noncanonical Lipopolysaccharide Binding to Bacterial Inner Membrane Proteins.

    Urner, Leonhard H / Fiorentino, Francesco / Shutin, Denis / Sauer, Joshua B / Agasid, Mark T / El-Baba, Tarick J / Bolla, Jani R / Stansfeld, Phillip J / Robinson, Carol V

    Journal of the American Chemical Society

    2024  

    Abstract: Lipopolysaccharide (LPS) is vital for maintaining the outer membrane barrier in Gram-negative bacteria. LPS is also frequently obtained in complex with the inner membrane proteins after detergent purification. The question of whether or not LPS binding ... ...

    Abstract Lipopolysaccharide (LPS) is vital for maintaining the outer membrane barrier in Gram-negative bacteria. LPS is also frequently obtained in complex with the inner membrane proteins after detergent purification. The question of whether or not LPS binding to inner membrane proteins not involved in outer membrane biogenesis reflects native lipid environments remains unclear. Here, we leverage the control of the hydrophilic-lipophilic balance and packing parameter concepts to chemically tune detergents that can be used to qualitatively differentiate the degree to which proteins copurify with phospholipids (PLs) and/or LPS. Given the scalable properties of these detergents, we demonstrate a detergent fine-tuning that enables the facile investigation of intact proteins and their complexes with lipids by native mass spectrometry (nMS). We conclude that LPS, a lipid that is believed to be important for outer membranes, can also affect the activity of membrane proteins that are currently not assigned to be involved in outer membrane biogenesis. Our results deliver a scalable detergent chemistry for a streamlined biophysical characterization of protein-lipid interactions, provide a rationale for the high affinity of LPS-protein binding, and identify noncanonical associations between LPS and inner membrane proteins with relevance for membrane biology and antibiotic research.
    Language English
    Publishing date 2024-04-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c14358
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Multi-responsive hydrogel structures from patterned droplet networks.

    Downs, Florence G / Lunn, David J / Booth, Michael J / Sauer, Joshua B / Ramsay, William J / Klemperer, R George / Hawker, Craig J / Bayley, Hagan

    Nature chemistry

    2020  Volume 12, Issue 4, Page(s) 363–371

    Abstract: Responsive hydrogels that undergo controlled shape changes in response to a range of stimuli are of interest for microscale soft robotic and biomedical devices. However, these applications require fabrication methods capable of preparing complex, ... ...

    Abstract Responsive hydrogels that undergo controlled shape changes in response to a range of stimuli are of interest for microscale soft robotic and biomedical devices. However, these applications require fabrication methods capable of preparing complex, heterogeneous materials. Here we report a new approach for making patterned, multi-material and multi-responsive hydrogels, on a micrometre to millimetre scale. Nanolitre aqueous pre-gel droplets were connected through lipid bilayers in predetermined architectures and photopolymerized to yield continuous hydrogel structures. By using this droplet network technology to pattern domains containing temperature-responsive or non-responsive hydrogels, structures that undergo reversible curling were produced. Through patterning of gold nanoparticle-containing domains into the hydrogels, light-activated shape change was achieved, while domains bearing magnetic particles allowed movement of the structures in a magnetic field. To highlight our technique, we generated a multi-responsive hydrogel that, at one temperature, could be moved through a constriction under a magnetic field and, at a second temperature, could grip and transport a cargo.
    Language English
    Publishing date 2020-03-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2464596-5
    ISSN 1755-4349 ; 1755-4330
    ISSN (online) 1755-4349
    ISSN 1755-4330
    DOI 10.1038/s41557-020-0444-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Direct observation of the influence of cardiolipin and antibiotics on lipid II binding to MurJ.

    Bolla, Jani Reddy / Sauer, Joshua B / Wu, Di / Mehmood, Shahid / Allison, Timothy M / Robinson, Carol V

    Nature chemistry

    2018  Volume 10, Issue 3, Page(s) 363–371

    Abstract: Translocation of lipid II across the cytoplasmic membrane is essential in peptidoglycan biogenesis. Although most steps are understood, identifying the lipid II flippase has yielded conflicting results, and the lipid II binding properties of two ... ...

    Abstract Translocation of lipid II across the cytoplasmic membrane is essential in peptidoglycan biogenesis. Although most steps are understood, identifying the lipid II flippase has yielded conflicting results, and the lipid II binding properties of two candidate flippases-MurJ and FtsW-remain largely unknown. Here we apply native mass spectrometry to both proteins and characterize lipid II binding. We observed lower levels of lipid II binding to FtsW compared to MurJ, consistent with MurJ having a higher affinity. Site-directed mutagenesis of MurJ suggests that mutations at A29 and D269 attenuate lipid II binding to MurJ, whereas chemical modification of A29 eliminates binding. The antibiotic ramoplanin dissociates lipid II from MurJ, whereas vancomycin binds to form a stable complex with MurJ:lipid II. Furthermore, we reveal cardiolipins associate with MurJ but not FtsW, and exogenous cardiolipins reduce lipid II binding to MurJ. These observations provide insights into determinants of lipid II binding to MurJ and suggest roles for endogenous lipids in regulating substrate binding.
    MeSH term(s) Anti-Bacterial Agents/chemistry ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Binding Sites ; Cardiolipins/chemistry ; Cardiolipins/metabolism ; Depsipeptides/chemistry ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Mass Spectrometry ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Mutagenesis, Site-Directed ; Phospholipid Transfer Proteins/chemistry ; Phospholipid Transfer Proteins/genetics ; Phospholipid Transfer Proteins/metabolism ; Uridine Diphosphate N-Acetylmuramic Acid/analogs & derivatives ; Uridine Diphosphate N-Acetylmuramic Acid/chemistry
    Chemical Substances Anti-Bacterial Agents ; Bacterial Proteins ; Cardiolipins ; Depsipeptides ; Escherichia coli Proteins ; Membrane Proteins ; MurJ protein, E coli ; Phospholipid Transfer Proteins ; Uridine Diphosphate N-Acetylmuramic Acid ; muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol ; ramoplanin (0WX9996O2G) ; FtsW protein, Bacteria (125724-13-2)
    Language English
    Publishing date 2018-01-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2464596-5
    ISSN 1755-4349 ; 1755-4330
    ISSN (online) 1755-4349
    ISSN 1755-4330
    DOI 10.1038/nchem.2919
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Dynamics of an LPS translocon induced by substrate and an antimicrobial peptide.

    Fiorentino, Francesco / Sauer, Joshua B / Qiu, Xingyu / Corey, Robin A / Cassidy, C Keith / Mynors-Wallis, Benjamin / Mehmood, Shahid / Bolla, Jani R / Stansfeld, Phillip J / Robinson, Carol V

    Nature chemical biology

    2020  Volume 17, Issue 2, Page(s) 187–195

    Abstract: Lipopolysaccharide (LPS) transport to the outer membrane (OM) is a crucial step in the biogenesis of microbial surface defenses. Although many features of the translocation mechanism have been elucidated, molecular details of LPS insertion via the LPS ... ...

    Abstract Lipopolysaccharide (LPS) transport to the outer membrane (OM) is a crucial step in the biogenesis of microbial surface defenses. Although many features of the translocation mechanism have been elucidated, molecular details of LPS insertion via the LPS transport (Lpt) OM protein LptDE remain elusive. Here, we integrate native MS with hydrogen-deuterium exchange MS and molecular dynamics simulations to investigate the influence of substrate and peptide binding on the conformational dynamics of LptDE. Our data reveal that LPS induces opening of the LptD β-taco domain, coupled with conformational changes on β-strands adjacent to the putative lateral exit gate. Conversely, an antimicrobial peptide, thanatin, stabilizes the β-taco, thereby preventing LPS transport. Our results illustrate that LPS insertion into the OM relies on concerted opening movements of both the β-barrel and β-taco domains of LptD, and suggest a means for developing antimicrobial therapeutics targeting this essential process in Gram-negative ESKAPE pathogens.
    MeSH term(s) Anti-Bacterial Agents/pharmacology ; Antimicrobial Cationic Peptides/pharmacology ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Outer Membrane Proteins/metabolism ; Carbohydrate Conformation ; Drug Resistance, Bacterial/genetics ; Gram-Negative Bacteria/drug effects ; Gram-Negative Bacteria/genetics ; Klebsiella pneumoniae/genetics ; Klebsiella pneumoniae/metabolism ; Lipopolysaccharides/metabolism ; Mass Spectrometry ; Models, Molecular ; Molecular Dynamics Simulation ; Translocation, Genetic/genetics
    Chemical Substances Anti-Bacterial Agents ; Antimicrobial Cationic Peptides ; Bacterial Outer Membrane Proteins ; Lipopolysaccharides ; thanatin
    Language English
    Publishing date 2020-11-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-020-00694-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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