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Journal articles on the topic 'Gram-negative inner membrane'

Author: Grafiati

Published: 6 September 2023

Last updated: 7 September 2023

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1

Powers, Matthew J., and M. Stephen Trent. "Intermembrane transport: Glycerophospholipid homeostasis of the Gram-negative cell envelope." Proceedings of the National Academy of Sciences 116, no. 35 (2019): 17147–55. http://dx.doi.org/10.1073/pnas.1902026116.

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This perspective addresses recent advances in lipid transport across the Gram-negative inner and outer membranes. While we include a summary of previously existing literature regarding this topic, we focus on the maintenance of lipid asymmetry (Mla) pathway. Discovered in 2009 by the Silhavy group [J. C. Malinverni, T. J. Silhavy, Proc. Natl. Acad. Sci. U.S.A. 106, 8009–8014 (2009)], Mla has become increasingly appreciated for its role in bacterial cell envelope physiology. Through the work of many, we have gained an increasingly mechanistic understanding of the function of Mla via genetic, bi

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Orlando, Benjamin, Yanyan Li, and Maofu Liao. "Snapshots of Endotoxin Extraction from the Gram-negative Inner Membrane." Microscopy and Microanalysis 26, S2 (2020): 2520. http://dx.doi.org/10.1017/s1431927620021893.

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Epand, Raquel F., Jake E. Pollard, Jonathan O. Wright, Paul B. Savage, and Richard M. Epand. "Depolarization, Bacterial Membrane Composition, and the Antimicrobial Action of Ceragenins." Antimicrobial Agents and Chemotherapy 54, no. 9 (2010): 3708–13. http://dx.doi.org/10.1128/aac.00380-10.

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ABSTRACT Ceragenins are cholic acid-derived antimicrobial agents that mimic the activity of endogenous antimicrobial peptides. Ceragenins target bacterial membranes, yet the consequences of these interactions have not been fully elucidated. The role of the outer membrane in allowing access of the ceragenins to the cytoplasmic membrane of Gram-negative bacteria was studied using the ML-35p mutant strain of Escherichia coli that has been engineered to allow independent monitoring of small-molecule flux across the inner and outer membranes. The ceragenins CSA-8, CSA-13, and CSA-54 permeabilize th

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Sutterlin, Holly A., Handuo Shi, Kerrie L. May, et al. "Disruption of lipid homeostasis in the Gram-negative cell envelope activates a novel cell death pathway." Proceedings of the National Academy of Sciences 113, no. 11 (2016): E1565—E1574. http://dx.doi.org/10.1073/pnas.1601375113.

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Gram-negative bacteria balance synthesis of the outer membrane (OM), cell wall, and cytoplasmic contents during growth via unknown mechanisms. Here, we show that a dominant mutation (designatedmlaA*, maintenance of lipid asymmetry) that alters MlaA, a lipoprotein that removes phospholipids from the outer leaflet of the OM ofEscherichia coli, increases OM permeability, lipopolysaccharide levels, drug sensitivity, and cell death in stationary phase. Surprisingly, single-cell imaging revealed that death occurs after protracted loss of OM material through vesiculation and blebbing at cell-division

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Li, Xiangyuan, Lei Fu, Shan Zhang, Yipeng Wang, and Lianghui Gao. "How Alligator Immune Peptides Kill Gram-Negative Bacteria: A Lipid-Scrambling, Squeezing, and Extracting Mechanism Revealed by Theoretical Simulations." International Journal of Molecular Sciences 24, no. 13 (2023): 10962. http://dx.doi.org/10.3390/ijms241310962.

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Alligator sinensis cathelicidins (As-CATHs) are antimicrobial peptides extracted from alligators that enable alligators to cope with diseases caused by bacterial infections. This study assessed the damaging effects of sequence-truncated and residue-substituted variants of As-CATH4, AS4-1, AS4-5, and AS4-9 (with decreasing charges but increasing hydrophobicity) on the membranes of Gram-negative bacteria at the molecular level by using coarse-grained molecular dynamics simulations. The simulations predicted that all the variants disrupt the structures of the inner membrane of Gram-negative bacte

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Pérez-Cruz, Carla, Lidia Delgado, Carmen López-Iglesias, and Elena Mercade. "Outer-Inner Membrane Vesicles Naturally Secreted by Gram-Negative Pathogenic Bacteria." PLOS ONE 10, no. 1 (2015): e0116896. http://dx.doi.org/10.1371/journal.pone.0116896.

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7

Raina, Satish. "Lipopolysaccharides: Regulated Biosynthesis and Structural Diversity." International Journal of Molecular Sciences 24, no. 8 (2023): 7498. http://dx.doi.org/10.3390/ijms24087498.

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The cell envelope of Gram-negative bacteria contains two distinct membranes, an inner (IM) and an outer (OM) membrane, separated by the periplasm, a hydrophilic compartment that includes a thin layer of peptidoglycan [...]

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Makowski, Marcin, Mário R. Felício, Isabel C. M. Fensterseifer, Octávio L. Franco, Nuno C. Santos, and Sónia Gonçalves. "EcDBS1R4, an Antimicrobial Peptide Effective against Escherichia coli with In Vitro Fusogenic Ability." International Journal of Molecular Sciences 21, no. 23 (2020): 9104. http://dx.doi.org/10.3390/ijms21239104.

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Discovering antibiotic molecules able to hold the growing spread of antimicrobial resistance is one of the most urgent endeavors that public health must tackle. The case of Gram-negative bacterial pathogens is of special concern, as they are intrinsically resistant to many antibiotics, due to an outer membrane that constitutes an effective permeability barrier. Antimicrobial peptides (AMPs) have been pointed out as potential alternatives to conventional antibiotics, as their main mechanism of action is membrane disruption, arguably less prone to elicit resistance in pathogens. Here, we investi

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Banack, Trevor, Peter D. Kim, and William Firshein. "TrfA-Dependent Inner Membrane-Associated Plasmid RK2 DNA Synthesis and Association of TrfA with Membranes of Different Gram-Negative Hosts." Journal of Bacteriology 182, no. 16 (2000): 4380–83. http://dx.doi.org/10.1128/jb.182.16.4380-4383.2000.

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ABSTRACT TrfA, the replication initiator protein of broad-host-range plasmid RK2, was tested for its ability to bind to the membrane of four different gram-negative hosts in addition to Escherichia coli: Pseudomonas aeruginosa, Pseudomonas putida, Salmonella enterica serovar Typhimurium, andRhodobacter sphaeroides. Cells harboring TrfA-encoding plasmids were fractionated into soluble, inner membrane, and outer membrane fractions. The fractions were subjected to Western blotting, and the blots were probed with antibody to the TrfA proteins. TrfA was found to fractionate with the cell membranes

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10

Clausell, Adrià, Maria Garcia-Subirats, Montserrat Pujol, M. Antonia Busquets, Francesc Rabanal, and Yolanda Cajal. "Gram-Negative Outer and Inner Membrane Models: Insertion of Cyclic Cationic Lipopeptides." Journal of Physical Chemistry B 111, no. 3 (2007): 551–63. http://dx.doi.org/10.1021/jp064757+.

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11

Jordan, L. D., Y. Zhou, C. R. Smallwood, et al. "Energy-dependent motion of TonB in the Gram-negative bacterial inner membrane." Proceedings of the National Academy of Sciences 110, no. 28 (2013): 11553–58. http://dx.doi.org/10.1073/pnas.1304243110.

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Marx, Lisa, Enrico Semeraro, Karl Lohner, and Georg Pabst. "Structural Properties of Inner and Outer Membrane Mimics of Gram-Negative Bacteria." Biophysical Journal 116, no. 3 (2019): 87a. http://dx.doi.org/10.1016/j.bpj.2018.11.512.

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13

Clifton, Luke A., Maximilian W. A. Skoda, Emma L. Daulton, et al. "Asymmetric phospholipid: lipopolysaccharide bilayers; a Gram-negative bacterial outer membrane mimic." Journal of The Royal Society Interface 10, no. 89 (2013): 20130810. http://dx.doi.org/10.1098/rsif.2013.0810.

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The Gram-negative bacterial outer membrane (OM) is a complex and highly asymmetric biological barrier but the small size of bacteria has hindered advances in in vivo examination of membrane dynamics. Thus, model OMs, amenable to physical study, are important sources of data. Here, we present data from asymmetric bilayers which emulate the OM and are formed by a simple two-step approach. The bilayers were deposited on an SiO 2 surface by Langmuir–Blodgett deposition of phosphatidylcholine as the inner leaflet and, via Langmuir–Schaefer deposition, an outer leaflet of either Lipid A or Escherich

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Cochrane, Stephen A., Brandon Findlay, Alireza Bakhtiary, et al. "Antimicrobial lipopeptide tridecaptin A1selectively binds to Gram-negative lipid II." Proceedings of the National Academy of Sciences 113, no. 41 (2016): 11561–66. http://dx.doi.org/10.1073/pnas.1608623113.

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Tridecaptin A1(TriA1) is a nonribosomal lipopeptide with selective antimicrobial activity against Gram-negative bacteria. Here we show that TriA1exerts its bactericidal effect by binding to the bacterial cell-wall precursor lipid II on the inner membrane, disrupting the proton motive force. Biochemical and biophysical assays show that binding to the Gram-negative variant of lipid II is required for membrane disruption and that only the proton gradient is dispersed. The NMR solution structure of TriA1in dodecylphosphocholine micelles with lipid II has been determined, and molecular modeling was

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Dombach, Jamie L., Joaquin L. J. Quintana, Toni A. Nagy, et al. "A small molecule that mitigates bacterial infection disrupts Gram-negative cell membranes and is inhibited by cholesterol and neutral lipids." PLOS Pathogens 16, no. 12 (2020): e1009119. http://dx.doi.org/10.1371/journal.ppat.1009119.

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Infections caused by Gram-negative bacteria are difficult to fight because these pathogens exclude or expel many clinical antibiotics and host defense molecules. However, mammals have evolved a substantial immune arsenal that weakens pathogen defenses, suggesting the feasibility of developing therapies that work in concert with innate immunity to kill Gram-negative bacteria. Using chemical genetics, we recently identified a small molecule, JD1, that kills Salmonella enterica serovar Typhimurium (S. Typhimurium) residing within macrophages. JD1 is not antibacterial in standard microbiological m

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Vetterli, Stefan U., Katja Zerbe, Maik Müller, et al. "Thanatin targets the intermembrane protein complex required for lipopolysaccharide transport inEscherichia coli." Science Advances 4, no. 11 (2018): eaau2634. http://dx.doi.org/10.1126/sciadv.aau2634.

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With the increasing resistance of many Gram-negative bacteria to existing classes of antibiotics, identifying new paradigms in antimicrobial discovery is an important research priority. Of special interest are the proteins required for the biogenesis of the asymmetric Gram-negative bacterial outer membrane (OM). Seven Lpt proteins (LptA to LptG) associate in most Gram-negative bacteria to form a macromolecular complex spanning the entire envelope, which transports lipopolysaccharide (LPS) molecules from their site of assembly at the inner membrane to the cell surface, powered by adenosine 5′-t

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Zaknoon, Fadia, Keren Goldberg, Hadar Sarig, Raquel F. Epand, Richard M. Epand, and Amram Mor. "Antibacterial Properties of an Oligo-Acyl-Lysyl Hexamer Targeting Gram-Negative Species." Antimicrobial Agents and Chemotherapy 56, no. 9 (2012): 4827–32. http://dx.doi.org/10.1128/aac.00511-12.

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ABSTRACTToward developing new tools for fighting resistance to antibiotics, we investigated the antibacterial properties of a new decanoyl-based oligo-acyl-lysyl (OAK) hexamer, aminododecanoyl-lysyl-[aminodecanoyl-lysyl]5(α12-5α10). The OAK exhibited preferential activity against Gram-negative bacteria (GNB), as determined using 36 strains, including diverse species, with an MIC90of 6.2 μM. The OAK's bactericidal mode of action was associated with rapid membrane depolarization and cell permeabilization, suggesting that the inner membrane was the primary target, whereas the observed binding aff

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18

Weerakoon, Dhanushka, Jan K. Marzinek, Peter J. Bond, Conrado Pedebos, and Syma Khalid. "Interactions of polymyxin B1 with the gram-negative inner membrane: A simulation study." Biophysical Journal 122, no. 3 (2023): 371a. http://dx.doi.org/10.1016/j.bpj.2022.11.2043.

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19

Dong, Haohao, Xiaodi Tang, Zhengyu Zhang, and Changjiang Dong. "Structural insight into lipopolysaccharide transport from the Gram-negative bacterial inner membrane to the outer membrane." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1862, no. 11 (2017): 1461–67. http://dx.doi.org/10.1016/j.bbalip.2017.08.003.

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McLeod, Sarah M., Paul R. Fleming, Kathleen MacCormack, et al. "Small-Molecule Inhibitors of Gram-Negative Lipoprotein Trafficking Discovered by Phenotypic Screening." Journal of Bacteriology 197, no. 6 (2015): 1075–82. http://dx.doi.org/10.1128/jb.02352-14.

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In Gram-negative bacteria, lipoproteins are transported to the outer membrane by the Lol system. In this process, lipoproteins are released from the inner membrane by the ABC transporter LolCDE and passed to LolA, a diffusible periplasmic molecular chaperone. Lipoproteins are then transferred to the outer membrane receptor protein, LolB, for insertion in the outer membrane. Here we describe the discovery and characterization of novel pyridineimidazole compounds that inhibit this process.Escherichia colimutants resistant to the pyridineimidazoles show no cross-resistance to other classes of ant

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Klebba, Phillip E. "ROSET Model of TonB Action in Gram-Negative Bacterial Iron Acquisition." Journal of Bacteriology 198, no. 7 (2016): 1013–21. http://dx.doi.org/10.1128/jb.00823-15.

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Therotationalsurveillance andenergytransfer (ROSET) model of TonB action suggests a mechanism by which the electrochemical proton gradient across the Gram-negative bacterial inner membrane (IM) promotes the transport of iron through ligand-gated porins (LGP) in the outer membrane (OM). TonB associates with the IM by an N-terminal hydrophobic helix that forms a complex with ExbBD. It also contains a central extended length of rigid polypeptide that spans the periplasm and a dimericC-terminal-ββαβ-domain (CTD) with LysM motifs that binds the peptidoglycan (PG) layer beneath the OM bilayer. The T

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Py, Béatrice, Laurent Loiseau, and Frédéric Barras. "An inner membrane platform in the type II secretion machinery of Gram‐negative bacteria." EMBO reports 2, no. 3 (2001): 244–48. http://dx.doi.org/10.1093/embo-reports/kve042.

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23

Simpson, Brent W., Janine M. May, David J. Sherman, Daniel Kahne, and Natividad Ruiz. "Lipopolysaccharide transport to the cell surface: biosynthesis and extraction from the inner membrane." Philosophical Transactions of the Royal Society B: Biological Sciences 370, no. 1679 (2015): 20150029. http://dx.doi.org/10.1098/rstb.2015.0029.

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The cell surface of most Gram-negative bacteria is covered with lipopolysaccharide (LPS). The network of charges and sugars provided by the dense packing of LPS molecules in the outer leaflet of the outer membrane interferes with the entry of hydrophobic compounds into the cell, including many antibiotics. In addition, LPS can be recognized by the immune system and plays a crucial role in many interactions between bacteria and their animal hosts. LPS is synthesized in the inner membrane of Gram-negative bacteria, so it must be transported across their cell envelope to assemble at the cell surf

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Josts, Inokentijs, Katharina Veith, Vincent Normant, Isabelle J. Schalk, and Henning Tidow. "Structural insights into a novel family of integral membrane siderophore reductases." Proceedings of the National Academy of Sciences 118, no. 34 (2021): e2101952118. http://dx.doi.org/10.1073/pnas.2101952118.

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Gram-negative bacteria take up the essential ion Fe3+ as ferric-siderophore complexes through their outer membrane using TonB-dependent transporters. However, the subsequent route through the inner membrane differs across many bacterial species and siderophore chemistries and is not understood in detail. Here, we report the crystal structure of the inner membrane protein FoxB (from Pseudomonas aeruginosa) that is involved in Fe-siderophore uptake. The structure revealed a fold with two tightly bound heme molecules. In combination with in vitro reduction assays and in vivo iron uptake studies,

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Pérez-Cruz, Carla, Ornella Carrión, Lidia Delgado, Gemma Martinez, Carmen López-Iglesias, and Elena Mercade. "New Type of Outer Membrane Vesicle Produced by the Gram-Negative Bacterium Shewanella vesiculosa M7T: Implications for DNA Content." Applied and Environmental Microbiology 79, no. 6 (2013): 1874–81. http://dx.doi.org/10.1128/aem.03657-12.

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ABSTRACTOuter membrane vesicles (OMVs) from Gram-negative bacteria are known to be involved in lateral DNA transfer, but the presence of DNA in these vesicles has remained difficult to explain. An ultrastructural study of the Antarctic psychrotolerant bacteriumShewanella vesiculosaM7Thas revealed that this Gram-negative bacterium naturally releases conventional one-bilayer OMVs through a process in which the outer membrane is exfoliated and only the periplasm is entrapped, together with a more complex type of OMV, previously undescribed, which on formation drag along inner membrane and cytopla

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Douglass, Martin V., François Cléon, and M. Stephen Trent. "Cardiolipin aids in lipopolysaccharide transport to the gram-negative outer membrane." Proceedings of the National Academy of Sciences 118, no. 15 (2021): e2018329118. http://dx.doi.org/10.1073/pnas.2018329118.

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In Escherichia coli, cardiolipin (CL) is the least abundant of the three major glycerophospholipids in the gram-negative cell envelope. However, E. coli harbors three distinct enzymes that synthesize CL: ClsA, ClsB, and ClsC. This redundancy suggests that CL is essential for bacterial fitness, yet CL-deficient bacteria are viable. Although multiple CL–protein interactions have been identified, the role of CL still remains unclear. To identify genes that impact fitness in the absence of CL, we analyzed high-density transposon (Tn) mutant libraries in combinatorial CL synthase mutant backgrounds

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Huntley, Jason F., Patrick G. Conley, Kayla E. Hagman, and Michael V. Norgard. "Characterization of Francisella tularensis Outer Membrane Proteins." Journal of Bacteriology 189, no. 2 (2006): 561–74. http://dx.doi.org/10.1128/jb.01505-06.

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ABSTRACT Francisella tularensis is a gram-negative coccobacillus that is capable of causing severe, fatal disease in a number of mammalian species, including humans. Little is known about the proteins that are surface exposed on the outer membrane (OM) of F. tularensis, yet identification of such proteins is potentially fundamental to understanding the initial infection process, intracellular survival, virulence, immune evasion and, ultimately, vaccine development. To facilitate the identification of putative F. tularensis outer membrane proteins (OMPs), the genomes of both the type A strain (

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Maktabi, Sepehr, Jeffrey W. Schertzer, and Paul R. Chiarot. "Dewetting-induced formation and mechanical properties of synthetic bacterial outer membrane models (GUVs) with controlled inner-leaflet lipid composition." Soft Matter 15, no. 19 (2019): 3938–48. http://dx.doi.org/10.1039/c9sm00223e.

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Kim, Jin-Young, Seong-Cheol Park, Moon-Young Yoon, Kyung-Soo Hahm, and Yoonkyung Park. "C-terminal amidation of PMAP-23: translocation to the inner membrane of Gram-negative bacteria." Amino Acids 40, no. 1 (2010): 183–95. http://dx.doi.org/10.1007/s00726-010-0632-1.

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Ma, Miao, Margaux Lustig, Michèle Salem, Dominique Mengin-Lecreulx, Gilles Phan, and Isabelle Broutin. "MexAB-OprM Efflux Pump Interaction with the Peptidoglycan of Escherichia coli and Pseudomonas aeruginosa." International Journal of Molecular Sciences 22, no. 10 (2021): 5328. http://dx.doi.org/10.3390/ijms22105328.

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One of the major families of membrane proteins found in prokaryote genome corresponds to the transporters. Among them, the resistance-nodulation-cell division (RND) transporters are highly studied, as being responsible for one of the most problematic mechanisms used by bacteria to resist to antibiotics, i.e., the active efflux of drugs. In Gram-negative bacteria, these proteins are inserted in the inner membrane and form a tripartite assembly with an outer membrane factor and a periplasmic linker in order to cross the two membranes to expulse molecules outside of the cell. A lot of information

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Berger, Carolin, Guillaume P. Robin, Ulla Bonas, and Ralf Koebnik. "Membrane topology of conserved components of the type III secretion system from the plant pathogen Xanthomonas campestris pv. vesicatoria." Microbiology 156, no. 7 (2010): 1963–74. http://dx.doi.org/10.1099/mic.0.039248-0.

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Type III secretion (T3S) systems play key roles in the assembly of flagella and the translocation of bacterial effector proteins into eukaryotic host cells. Eleven proteins which are conserved among Gram-negative plant and animal pathogenic bacteria have been proposed to build up the basal structure of the T3S system, which spans both inner and outer bacterial membranes. We studied six conserved proteins, termed Hrc, predicted to reside in the inner membrane of the plant pathogen Xanthomonas campestris pv. vesicatoria. The membrane topology of HrcD, HrcR, HrcS, HrcT, HrcU and HrcV was studied

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Zhang, Ge, Vadim Baidin, Karanbir S. Pahil, et al. "Cell-based screen for discovering lipopolysaccharide biogenesis inhibitors." Proceedings of the National Academy of Sciences 115, no. 26 (2018): 6834–39. http://dx.doi.org/10.1073/pnas.1804670115.

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New drugs are needed to treat gram-negative bacterial infections. These bacteria are protected by an outer membrane which prevents many antibiotics from reaching their cellular targets. The outer leaflet of the outer membrane contains LPS, which is responsible for creating this permeability barrier. Interfering with LPS biogenesis affects bacterial viability. We developed a cell-based screen that identifies inhibitors of LPS biosynthesis and transport by exploiting the nonessentiality of this pathway inAcinetobacter. We used this screen to find an inhibitor of MsbA, an ATP-dependent flippase t

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Li, Shiqi, Ruohua Ren, Letian Lyu, et al. "Solid and Liquid Surface-Supported Bacterial Membrane Mimetics as a Platform for the Functional and Structural Studies of Antimicrobials." Membranes 12, no. 10 (2022): 906. http://dx.doi.org/10.3390/membranes12100906.

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Increasing antibiotic resistance has provoked the urgent need to investigate the interactions of antimicrobials with bacterial membranes. The reasons for emerging antibiotic resistance and innovations in novel therapeutic approaches are highly relevant to the mechanistic interactions between antibiotics and membranes. Due to the dynamic nature, complex compositions, and small sizes of native bacterial membranes, bacterial membrane mimetics have been developed to allow for the in vitro examination of structures, properties, dynamics, and interactions. In this review, three types of model membra

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Segovia, Roser, Judith Solé, Ana Maria Marqués, Yolanda Cajal, and Francesc Rabanal. "Unveiling the Membrane and Cell Wall Action of Antimicrobial Cyclic Lipopeptides: Modulation of the Spectrum of Activity." Pharmaceutics 13, no. 12 (2021): 2180. http://dx.doi.org/10.3390/pharmaceutics13122180.

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Antibiotic resistance is a major public health challenge, and Gram-negative multidrug-resistant bacteria are particularly dangerous. The threat of running out of active molecules is accelerated by the extensive use of antibiotics in the context of the COVID-19 pandemic, and new antibiotics are urgently needed. Colistin and polymyxin B are natural antibiotics considered as last resort drugs for multi-resistant infections, but their use is limited because of neuro- and nephrotoxicity. We previously reported a series of synthetic analogues inspired in natural polymyxins with a flexible scaffold t

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Nguyen, Hang Thi, Lisa A. O’Donovan, Henrietta Venter, et al. "Comparison of Two Transmission Electron Microscopy Methods to Visualize Drug-Induced Alterations of Gram-Negative Bacterial Morphology." Antibiotics 10, no. 3 (2021): 307. http://dx.doi.org/10.3390/antibiotics10030307.

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In this study, we optimized and compared different transmission electron microscopy (TEM) methods to visualize changes to Gram-negative bacterial morphology induced by treatment with a robenidine analogue (NCL195) and colistin combination. Aldehyde-fixed bacterial cells (untreated, treated with colistin or NCL195 + colistin) were prepared using conventional TEM methods and compared with ultrathin Tokuyasu cryo-sections. The results of this study indicate superiority of ultrathin cryo-sections in visualizing the membrane ultrastructure of Escherichia coli and Pseudomonas aeruginosa, with a clea

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Xu, Yongbin, Arne Moeller, So-Young Jun, et al. "Assembly and Channel Opening of Outer Membrane Protein in Tripartite Drug Efflux Pumps of Gram-negative Bacteria." Journal of Biological Chemistry 287, no. 15 (2012): 11740–50. http://dx.doi.org/10.1074/jbc.m111.329375.

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Gram-negative bacteria are capable of expelling diverse xenobiotic substances from within the cell by use of three-component efflux pumps in which the energy-activated inner membrane transporter is connected to the outer membrane channel protein via the membrane fusion protein. In this work, we describe the crystal structure of the membrane fusion protein MexA from the Pseudomonas aeruginosa MexAB-OprM pump in the hexameric ring arrangement. Electron microscopy study on the chimeric complex of MexA and the outer membrane protein OprM reveals that MexA makes a tip-to-tip interaction with OprM,

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Gawarzewski, Iris, Sander H. J. Smits, Lutz Schmitt, and Joachim Jose. "Structural comparison of the transport units of type V secretion systems." Biological Chemistry 394, no. 11 (2013): 1385–98. http://dx.doi.org/10.1515/hsz-2013-0162.

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Abstract Pathogenic gram-negative bacteria have evolved several secretion mechanisms to translocate adhesins, enzymes, toxins, and other virulence factors across the inner and outer membranes. Currently, eight different secretion systems, type I–type VIII (T1SS–T8SS) plus the chaperone-usher (CU) pathway, have been identified, which act in one-step or two-step mechanisms to traverse both membrane barriers. The type V secretion system (T5SS) is dependent first on the Sec translocon within the inner membrane. The periplasmic intermediates are then secreted through aqueous pores formed by β-barre

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Samantarrai, Devyani, Annapoorni Lakshman Sagar, Ramurthy Gudla, and Dayananda Siddavattam. "TonB-Dependent Transporters in Sphingomonads: Unraveling Their Distribution and Function in Environmental Adaptation." Microorganisms 8, no. 3 (2020): 359. http://dx.doi.org/10.3390/microorganisms8030359.

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TonB-dependent transport system plays a critical role in the transport of nutrients across the energy-deprived outer membrane of Gram-negative bacteria. It contains a specialized outer membrane TonB-dependent transporter (TBDT) and energy generating (ExbB/ExbD) and transducing (TonB) inner membrane multi-protein complex, called TonB complex. Very few TonB complex protein-coding sequences exist in the genomes of Gram-negative bacteria. Interestingly, the TBDT coding alleles are phenomenally high, especially in the genomes of bacteria surviving in complex and stressful environments. Sphingomonad

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Bootsma, Hester J., Piet C. Aerts, George Posthuma та ін. "Moraxella (Branhamella)catarrhalis BRO β-Lactamase: a Lipoprotein of Gram-Positive Origin?" Journal of Bacteriology 181, № 16 (1999): 5090–93. http://dx.doi.org/10.1128/jb.181.16.5090-5093.1999.

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ABSTRACT In the past 20 years, BRO β-lactamase-producing Moraxella catarrhalis strains have emerged. We show that BRO is expressed as a 33-kDa lipoprotein associated with the inner leaflet of the outer membrane. To our knowledge, this is the first description of a lipidated β-lactamase in a gram-negative species.

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Sperandeo, Paola, Rachele Cescutti, Riccardo Villa, et al. "Characterization of lptA and lptB, Two Essential Genes Implicated in Lipopolysaccharide Transport to the Outer Membrane of Escherichia coli." Journal of Bacteriology 189, no. 1 (2006): 244–53. http://dx.doi.org/10.1128/jb.01126-06.

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ABSTRACT The outer membrane (OM) of gram-negative bacteria is an asymmetric lipid bilayer that protects the cell from toxic molecules. Lipopolysaccharide (LPS) is an essential component of the OM in most gram-negative bacteria, and its structure and biosynthesis are well known. Nevertheless, the mechanisms of transport and assembly of this molecule in the OM are poorly understood. To date, the only proteins implicated in LPS transport are MsbA, responsible for LPS flipping across the inner membrane, and the Imp/RlpB complex, involved in LPS targeting to the OM. Here, we present evidence that t

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Aronova, N. V., N. V. Pavlovich, M. V. Tsimbalistova, S. N. Golovin, and A. S. Anisimova. "The Role of Outer Membrane Vesicles of Agents of Particularly Dangerous Infections in the Pathogenesis and Immunogenesis of Infectious Process." Problems of Particularly Dangerous Infections, no. 4 (January 24, 2022): 6–15. http://dx.doi.org/10.21055/0370-1069-2021-4-6-15.

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The literature review is devoted to the modern concepts of the vesiculation phenomenon and its biological role in pathogenic bacteria – causative agents of particularly dangerous human infections. Data on the production, structure, composition, and functions of the outer membrane vesicles (OMV) of bacteria have been summarized. In recent years, the interest of researchers in the formation of spherical structures (so called bubbles or vesicles) from outer membrane of gram-negative bacteria has significantly increased. Such structures are surrounded by the double layer of a phospholipid membrane

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Chi, Ximin, Qiongxuan Fan, Yuanyuan Zhang, et al. "Structural mechanism of phospholipids translocation by MlaFEDB complex." Cell Research 30, no. 12 (2020): 1127–35. http://dx.doi.org/10.1038/s41422-020-00404-6.

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AbstractIn Gram-negative bacteria, phospholipids are major components of the inner membrane and the inner leaflet of the outer membrane, playing an essential role in forming the unique dual-membrane barrier to exclude the entry of most antibiotics. Understanding the mechanisms of phospholipid translocation between the inner and outer membrane represents one of the major challenges surrounding bacterial phospholipid homeostasis. The conserved MlaFEDB complex in the inner membrane functions as an ABC transporter to drive the translocation of phospholipids between the inner membrane and the perip

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Long, Feng, Chih-Chia Su, Hsiang-Ting Lei, Jani Reddy Bolla, Sylvia V. Do, and Edward W. Yu. "Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex." Philosophical Transactions of the Royal Society B: Biological Sciences 367, no. 1592 (2012): 1047–58. http://dx.doi.org/10.1098/rstb.2011.0203.

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Gram-negative bacteria frequently expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membranes. The three parts are the inner membrane, substrate-binding transporter (or pump); a periplasmic membrane fusion protein (MFP, or adaptor); and an outer membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. One such efflux system CusCBA is responsible for extruding biocidal Cu(I) and Ag(I) ions. We previously described the crystal structures of both the inner membrane transporter CusA and the MFP CusB o

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Lenders, Michael H. H., Sven Reimann, Sander H. J. Smits, and Lutz Schmitt. "Molecular insights into type I secretion systems." Biological Chemistry 394, no. 11 (2013): 1371–84. http://dx.doi.org/10.1515/hsz-2013-0171.

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Abstract Type 1 secretion systems are one of the main machineries in Gram-negative bacteria involved in the secretion of a wide range of substrates from the cytoplasm across the inner and outer membrane in one step to the extracellular space. The range of substrates varies from small proteins up to large surface layer proteins of about 900 kDa. Most of the substrates have a non-cleavable C-terminal secretion signal and so-called GG repeats that are able to bind calcium ions. The translocator complex is composed of a trimeric outer membrane protein that provides a pore in the outer membrane. A

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Awang, Tadsanee, Phoom Chairatana, Ranjit Vijayan, and Prapasiri Pongprayoon. "Evaluation of the Binding Mechanism of Human Defensin 5 in a Bacterial Membrane: A Simulation Study." International Journal of Molecular Sciences 22, no. 22 (2021): 12401. http://dx.doi.org/10.3390/ijms222212401.

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Human α-defensin 5 (HD5) is a host-defense peptide exhibiting broad-spectrum antimicrobial activity. The lipopolysaccharide (LPS) layer on the Gram-negative bacterial membrane acts as a barrier to HD5 insertion. Therefore, the pore formation and binding mechanism remain unclear. Here, the binding mechanisms at five positions along the bacterial membrane axis were investigated using Molecular Dynamics. (MD) simulations. We found that HD5 initially placed at positions 1 to 3 moved up to the surface, while HD5 positioned at 4 and 5 remained within the membrane interacting with the middle and inne

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Xiang, Quanju, Haiyan Wang, Zhongshan Wang, Yizheng Zhang, and Changjiang Dong. "Characterization of lipopolysaccharide transport protein complex." Open Life Sciences 9, no. 2 (2014): 131–38. http://dx.doi.org/10.2478/s11535-013-0250-5.

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AbstractLipopolysaccharide (LPS) is an essential component of the outer membranes (OM) of most Gram-negative bacteria, which plays a crucial role in protection of the bacteria from toxic compounds and harsh conditions. The LPS is biosynthesized at the cytoplasmic side of inner membrane (IM), and then transported across the aqueous periplasmic compartment and assembled correctly at the outer membrane. This process is accomplished by seven LPS transport proteins (LptA-G), but the transport mechanism remains poorly understood. Here, we present findings by pull down assays in which the periplasmic

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Mensa, Bruk, Yong Ho Kim, Sungwook Choi, Richard Scott, Gregory A. Caputo, and William F. DeGrado. "Antibacterial Mechanism of Action of Arylamide Foldamers." Antimicrobial Agents and Chemotherapy 55, no. 11 (2011): 5043–53. http://dx.doi.org/10.1128/aac.05009-11.

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ABSTRACTSmall arylamide foldamers designed to mimic the amphiphilic nature of antimicrobial peptides (AMPs) have shown potent bactericidal activity against both Gram-negative and Gram-positive strains without many of the drawbacks of natural AMPs. These foldamers were shown to cause large changes in the permeability of the outer membrane ofEscherichia coli. They cause more limited permeabilization of the inner membrane which reaches critical levels corresponding with the time required to bring about bacterial cell death. Transcriptional profiling ofE. colitreated with sublethal concentrations

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Urfer, Matthias, Jasmina Bogdanovic, Fabio Lo Monte, et al. "A Peptidomimetic Antibiotic Targets Outer Membrane Proteins and Disrupts Selectively the Outer Membrane in Escherichia coli." Journal of Biological Chemistry 291, no. 4 (2015): 1921–32. http://dx.doi.org/10.1074/jbc.m115.691725.

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Increasing antibacterial resistance presents a major challenge in antibiotic discovery. One attractive target in Gram-negative bacteria is the unique asymmetric outer membrane (OM), which acts as a permeability barrier that protects the cell from external stresses, such as the presence of antibiotics. We describe a novel β-hairpin macrocyclic peptide JB-95 with potent antimicrobial activity against Escherichia coli. This peptide exhibits no cellular lytic activity, but electron microscopy and fluorescence studies reveal an ability to selectively disrupt the OM but not the inner membrane of E.

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Tefsen, Boris, Martine P. Bos, Frank Beckers, Jan Tommassen, and Hans de Cock. "MsbA Is Not Required for Phospholipid Transport in Neisseria meningitidis." Journal of Biological Chemistry 280, no. 43 (2005): 35961–66. http://dx.doi.org/10.1074/jbc.m509026200.

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The outer membrane of Gram-negative bacteria contains phospholipids and lipopolysaccharide (LPS) in the inner and outer leaflet, respectively. Little is known about the transport of the phospholipids from their site of synthesis to the outer membrane. The inner membrane protein MsbA of Escherichia coli, which is involved in the transport of LPS across the inner membrane, has been reported to be involved in phospholipid transport as well. Here, we have reported the construction and the characterization of a Neisseria meningitidis msbA mutant. The mutant was viable, and it showed a retarded grow

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Kim, Peter D., and William Firshein. "Isolation of an Inner Membrane-Derived Subfraction That Supports In Vitro Replication of a Mini-RK2 Plasmid inEscherichia coli." Journal of Bacteriology 182, no. 6 (2000): 1757–60. http://dx.doi.org/10.1128/jb.182.6.1757-1760.2000.

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ABSTRACT Previous results have demonstrated that the inner, but not the outer, membrane fraction of Escherichia coli is the site of membrane-associated DNA replication of plasmid RK2, a broad-host-range plasmid capable of replication in a wide variety of gram-negative hosts (K. Michaels, J. Mei, and W. Firshein, Plasmid 32:19–31, 1994). To resolve the inner membrane replication site further, the procedure of Ishidate et al. (K. Ishidate, E. S. Creeger, J. Zrike, S. Deb, G. Glauner, T. J. MacAlister, and L. I. Rothfield, J. Biol. Chem. 261:428–443, 1986) was used to separate the inner membrane

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