Latex can coagulate itself by the bacteria attack its protein membrane, bacteria contain hydrogen ion that can neutralise negative ion .

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The type II secretion system: biogenesis, molecular architecture and mechanism.

Nat Rev Microbiol . 2012 Apr 2; Korotkov KV, Sandkvist M, Hol WG Many Gram-negative bacteria use the sophisticated type II secretion system (T2SS) to translocate a wide range of proteins from the periplasm across the outer membrane.

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The type II secretion system: biogenesis, molecular architecture and mechanism.

The Bacillus subtilis cannibalism toxin SDP collapses the proton motive force and induces autolysis.

Mol Microbiol . 2012 Apr 2; Lamsa A, Liu WT, Dorrestein PC, Pogliano K Bacillus subtilis SDP is a peptide toxin that kills cells outside the biofilm to support continued growth. We show that purified SDP acts like endogenously produced SDP; it delays sporulation, and the SdpI immunity protein confers SDP resistance

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The Bacillus subtilis cannibalism toxin SDP collapses the proton motive force and induces autolysis.

Yeast: Cell wall, nucleus, cytoplasm, cell membrane, mitochondria. Cell wall isn’t made of cellulose (for bacteria and yeast) but protein.

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Expression of membrane-associated proteins within single emulsion cell fascimiles.

Analyst. 2012 Mar 22;
Chanasakulniyom M, Martino C, Paterson D, Horsfall L, Rosser S, Cooper JM

MreB is a structural membrane-associated protein which is one of the key components of the bacterial cytoskeleton. Although it plays an important role in shape maintenance of rod-like bacteria, the understanding of its mechanism of action is still not fully understood. This study shows how segmented flow and microdroplet technology can be used as a new tool for biological in vitro investigation of this protein. In this paper, we demonstrate cell-free expression in a single emulsion system to express red fluorescence protein (RFP) and MreB linked RFP (MreB-RFP). We follow the aggregation and localisation of the fusion protein MreB-RFP in this artificial cell-like environment. The expression of MreB-RFP in single emulsion droplets leads to the formation of micrometer-scale protein patches distributed at the water/oil interface.

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Expression of membrane-associated proteins within single emulsion cell fascimiles.

Pasteurella Multocida and Immune Cells.

Curr Top Microbiol Immunol . 2012 Mar 20; Kubatzky KF Pasteurella multocida was first discovered by Perroncito in 1878 and named after Louis Pasteur who first isolated and described this Gram-negative bacterium as the cause of fowl disease in 1880. Subsequently, P.

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Pasteurella Multocida and Immune Cells.

Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex.

Philos Trans R Soc Lond B Biol Sci . 2012 Apr 19; 367(1592): 1047-58 Long F, Su CC, Lei HT, Bolla JR, Do SV, Yu EW 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.

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Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex.

On the path to uncover the bacterial type II secretion system.

Philos Trans R Soc Lond B Biol Sci . 2012 Apr 19; 367(1592): 1059-72 Douzi B, Filloux A, Voulhoux R Gram-negative bacteria have evolved several secretory pathways to release enzymes or toxins into the surrounding environment or into the target cells. The type II secretion system (T2SS) is conserved in Gram-negative bacteria and involves a set of 12 to 16 different proteins

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On the path to uncover the bacterial type II secretion system.

On the path to uncover the bacterial type II secretion system.

Philos Trans R Soc Lond B Biol Sci . 2012 Apr 19; 367(1592): 1059-72 Douzi B, Filloux A, Voulhoux R Gram-negative bacteria have evolved several secretory pathways to release enzymes or toxins into the surrounding environment or into the target cells. The type II secretion system (T2SS) is conserved in Gram-negative bacteria and involves a set of 12 to 16 different proteins

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On the path to uncover the bacterial type II secretion system.

Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane.

Philos Trans R Soc Lond B Biol Sci . 2012 Apr 19; 367(1592): 1088-101 Leo JC, Grin I, Linke D Autotransport in Gram-negative bacteria denotes the ability of surface-localized proteins to cross the outer membrane (OM) autonomously. Autotransporters perform this task with the help of a β-barrel transmembrane domain localized in the OM.

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Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane.

Circulating Bacterial Membrane Vesicles Cause Sepsis in Rats.

Shock . 2012 Mar 5; Shah B, Sullivan CJ, Lonergan NE, Stanley S, Soult MC, Britt LD ABSTRACT: Gram negative bacteria remain the leading cause of sepsis, a disease which is consistently in the top ten causes of death internationally. Curing bacteremia alone does not necessarily end the disease process as other factors may cause inflammatory damage

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Circulating Bacterial Membrane Vesicles Cause Sepsis in Rats.

Structural characterization and oligomerization of the TssL protein, a component shared by the bacterial Type VI and Type IVb secretion systems.

J Biol Chem . 2012 Feb 27; Durand E, Zoued A, Spinelli S, Watson PJ, Aschtgen MS, Journet L, Cambillau C, Cascales E The type VI secretion system (T6SS)4 is a macromolecular system distributed in Gram negative bacteria, responsible for the secretion of effector proteins into target cells. The T6SS has a broad versatility as it can target both eukaryotic and prokaryotic cells

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Structural characterization and oligomerization of the TssL protein, a component shared by the bacterial Type VI and Type IVb secretion systems.

Structural characterization and oligomerization of the TssL protein, a component shared by the bacterial Type VI and Type IVb secretion systems.

J Biol Chem . 2012 Feb 27; Durand E, Zoued A, Spinelli S, Watson PJ, Aschtgen MS, Journet L, Cambillau C, Cascales E The type VI secretion system (T6SS)4 is a macromolecular system distributed in Gram negative bacteria, responsible for the secretion of effector proteins into target cells. The T6SS has a broad versatility as it can target both eukaryotic and prokaryotic cells.

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Structural characterization and oligomerization of the TssL protein, a component shared by the bacterial Type VI and Type IVb secretion systems.

Structural characterization and oligomerization of the TssL protein, a component shared by the bacterial Type VI and Type IVb secretion systems.

J Biol Chem . 2012 Feb 27; Durand E, Zoued A, Spinelli S, Watson PJ, Aschtgen MS, Journet L, Cambillau C, Cascales E The type VI secretion system (T6SS)4 is a macromolecular system distributed in Gram negative bacteria, responsible for the secretion of effector proteins into target cells.

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Structural characterization and oligomerization of the TssL protein, a component shared by the bacterial Type VI and Type IVb secretion systems.

Characterization of HrpB2 from Xanthomonas campestris pv. vesicatoria identifies protein regions that are essential for type III secretion pilus formation.

Microbiology . 2012 Feb 16; Hartmann N, Schulz S, Lorenz C, Fraas S, Hause G, Buettner D The Gram-negative plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria employs a type III secretion (T3S) system to translocate effector proteins into plant cells

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Characterization of HrpB2 from Xanthomonas campestris pv. vesicatoria identifies protein regions that are essential for type III secretion pilus formation.

Structural and Functional Insights into the Pilotin-Secretin Complex of the Type II Secretion System.

PLoS Pathog . 2012 Feb; 8(2): e1002531 Gu S, Rehman S, Wang X, Shevchik VE, Pickersgill RW Gram-negative bacteria secrete virulence factors and assemble fibre structures on their cell surface using specialized secretion systems.

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Structural and Functional Insights into the Pilotin-Secretin Complex of the Type II Secretion System.