Crystal structure of the N-lobe of lactoferrin binding protein B from Moraxella bovis (1) () This paper is an invited article as a result of a presentation at the International Lactoferrin Conference held in Mazatlan, Mexico (May 2011), and has undergone the Journal’s usual peer review process.

Biochem Cell Biol . 2012 Feb 14; Arutyunova E, Brooks CL, Beddek A, Mak MW, Schryvers AB, Lemieux MJ Lactoferrin (Lf) is a bi-lobed, iron-binding protein found on mucosal surfaces and at sites of inflammation.

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Crystal structure of the N-lobe of lactoferrin binding protein B from Moraxella bovis (1) () This paper is an invited article as a result of a presentation at the International Lactoferrin Conference held in Mazatlan, Mexico (May 2011), and has undergone the Journal’s usual peer review process.

Construction and screening of attenuated ΔphoP/Q Salmonella typhimurium vectored plague vaccine candidates.

Hum Vaccin Immunother . 2012 Mar 1; 8(3): Sizemore D, Warner E, Lawrence J, Thomas LJ, Roland K, Killeen K Preclinical studies evaluating plague vaccine candidates have demonstrated that the F1 and V antigen proteins of Yersinia pestis provide protection against challenge from virulent strains. Live-attenuated ΔphoP/Q Salmonella typhimurium recombinants expressing either F1, V antigen, F1 plus V antigen, or a F1-V fusion from Asd (+) balanced-lethal plasmids were constructed

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Construction and screening of attenuated ΔphoP/Q Salmonella typhimurium vectored plague vaccine candidates.

Construction and screening of attenuated ΔphoP/Q Salmonella typhimurium vectored plague vaccine candidates.

Hum Vaccin Immunother . 2012 Mar 1; 8(3): Sizemore D, Warner E, Lawrence J, Thomas LJ, Roland K, Killeen K Preclinical studies evaluating plague vaccine candidates have demonstrated that the F1 and V antigen proteins of Yersinia pestis provide protection against challenge from virulent strains.

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Construction and screening of attenuated ΔphoP/Q Salmonella typhimurium vectored plague vaccine candidates.

Structural Characterization of Integral Membrane Proteins | JRF …

Applications are invited for the post of Junior Research Fellow (JRF) under a DST Project entitled “Structural Characterization of Integral Membrane Proteins with Proteolytic activity from Pathogenic Bacterial species” funded

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Structural Characterization of Integral Membrane Proteins | JRF …

Structural Characterization of Integral Membrane Proteins | JRF …

Applications are invited for the post of Junior Research Fellow (JRF) under a DST Project entitled “Structural Characterization of Integral Membrane Proteins with Proteolytic activity from Pathogenic Bacterial species” funded

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Structural Characterization of Integral Membrane Proteins | JRF …

doxycycline action: Thought to inhibit bacterial protein and to alter cytoplasmic membrane of susceptible organisms. …I actually get it

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doxycycline action: Thought to inhibit bacterial protein and to alter cytoplasmic membrane of susceptible organisms. …I actually get it

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Proteome Science | Abstract | Adaptation of Salmonella enterica …

a major cause of human gastroenteritis worldwide. Outer membrane proteins whose production is often regulated by environmental conditions also play important roles in the adaptability of bacterial pathogens to various environments. The present study investigated the adaptation of S. Hadar under the effect of acute static magnetic field exposure (200 mT, 9 h) and the impact on the outer membrane protein pattern. Via two-dimensional electrophoresis (2-DE) and

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Proteome Science | Abstract | Adaptation of Salmonella enterica …

Bacillus cereus can attack the cell membranes of the alga Chara corallina by means of HlyII.

Biochim Biophys Acta. 2012 Jan 17;
Kataev AA, Andreeva-Kovalevskaya ZI, Solonin AS, Ternovsky VI

We studied the influence of Bacillus cereus bacteria on cells of the freshwater alga Chara corallina. These bacteria and recombinant Bacillus subtilis strains are capable of producing the secreted toxin HlyII, which changes the electrophysiological parameters of the algal electrically excitable plasma membrane by forming pores. Cooperative incubation of bacterial cells, which carry active hlyII gene, and Chara corallina cells caused a decrease in the resting potential (V(m)) and plasma membrane resistance (R(m)) of algal cells. The efficiency of each strain was commensurable with its ability to produce HlyII. Purified hemolysin II caused a similar effect on V(m) and R(m) of intact and perfused cells. This protein changed the kinetics and magnitude of transient voltage-dependent calcium and calcium-activated chloride currents owing to the formation of additional Ca(2+)-permeable pores in algal cell membrane. Occurrence of the cellulose cell wall with pores 2.1 to 4.6nm in diameter suggests that HlyII molecules reach the plasma membrane surface strictly as monomers.

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Bacillus cereus can attack the cell membranes of the alga Chara corallina by means of HlyII.

The Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion.

Cell Host Microbe. 2012 Jan 19; 11(1): 46-57
Arasaki K, Toomre DK, Roy CR

The intracellular bacterial pathogen Legionella pneumophila subverts host membrane transport pathways to promote fusion of vesicles exiting the endoplasmic reticulum (ER) with the pathogen-containing vacuole. During infection there is noncanonical pairing of the SNARE protein Sec22b on ER-derived vesicles with plasma membrane (PM)-localized syntaxin proteins on the vacuole. We show that the L. pneumophila Rab1-targeting effector DrrA is sufficient to stimulate this noncanonical SNARE association and promote membrane fusion. DrrA activation of the Rab1 GTPase on PM-derived organelles stimulated the tethering of ER-derived vesicles with the PM-derived organelle, resulting in vesicle fusion through the pairing of Sec22b with the PM syntaxin proteins. Thus, the effector protein DrrA stimulates a host membrane transport pathway that enables ER-derived vesicles to remodel a PM-derived organelle, suggesting that Rab1 activation at the PM is sufficient to promote the recruitment and fusion of ER-derived vesicles.

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The Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion.

http://t.co/lGwpCWRJ Outer membrane protein A and OprF – Versatile roles in Gram-negative bacterial infections http://t.co/mivZDPlK

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Outer membrane protein A and OprF – Versatile roles in Gram-negative bacterial infections.

FEBS J . 2012 Jan 12; Krishnan S, Prasadarao NV Outer membrane protein A (OmpA) is an abundant protein of Escherichia coli and other enterobacteria with a multitude of functions.

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Outer membrane protein A and OprF – Versatile roles in Gram-negative bacterial infections.

Outer membrane protein A and OprF – Versatile roles in Gram-negative bacterial infections.

FEBS J . 2012 Jan 12; Krishnan S, Prasadarao NV Outer membrane protein A (OmpA) is an abundant protein of Escherichia coli and other enterobacteria with a multitude of functions.

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Outer membrane protein A and OprF – Versatile roles in Gram-negative bacterial infections.

Meningococcal Outer Membrane Protein NhhA Triggers Apoptosis in Macrophages.

PLoS One . 2012; 7(1): e29586 Sjölinder M, Altenbacher G, Hagner M, Sun W, Schedin-Weiss S, Sjölinder H Phagocytotic cells play a fundamental role in the defense against bacterial pathogens.

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Meningococcal Outer Membrane Protein NhhA Triggers Apoptosis in Macrophages.

Outer membrane protein A and OprF – Versatile roles in Gram-negative bacterial infections http://t.co/drfkMOrl

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Outer membrane protein A and OprF – Versatile roles in Gram-negative bacterial infections http://t.co/YhnjJsWU

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