Results 41 to 50 of about 8,609 (220)

Glabralysins, potential New β-pore-forming toxin family members from the schistosomiasis vector snail biomphalaria glabrata [PDF]

, 2020
Biomphalaria glabrata is a freshwater Planorbidae snail. In its environment, this mollusk faces numerous microorganisms or pathogens, and has developed sophisticated innate immune mechanisms to survive.
Crickmore, Neil, Duval, David, Galinier, Richard, Gourbal, Benjamin, Lassalle, Damien, Pinaud, Silvain, Tetreau, Guillaume   +6 more
core   +3 more sources

Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157:H7 [PDF]

Infection and Immunity, 1996
A hemolytic determinant of enterohemorrhagic Escherichia coli O157:H7 is encoded on a 90-kbp plasmid (pO157). This enterohemorrhagic E. coli toxin (Ehx) is a newly described RTX cytotoxin. The prototype RTX toxin is the E. coli hemolysin (Hly) associated with extraintestinal E. coli infections. We expressed Ehx from E.
M E, Bauer, R A, Welch
openaire   +2 more sources

A Large Repetitive RTX-Like Protein Mediates Water-Soaked Lesion Development, Leakage of Plant Cell Content and Host Colonization in the Pantoea stewartii subsp. stewartii Pathosystem

Molecular Plant-Microbe Interactions, 2015
Pantoea stewartii subsp. stewartii is the etiological agent of Stewart’s wilt and is a serious bacterial pathogen affecting sweet corn. During the leaf blight phase, P. stewartii colonizes the leaf apoplast and causes a characteristic water-soaked lesion.
M. Caroline Roper, Lindsey P. Burbank, Kayla Williams, Polrit Viravathana, Hsin-Yu Tien, Susanne von Bodman   +5 more
doaj   +1 more source

In vivo testing of novel vaccine prototypes against Actinobacillus pleuropneumoniae [PDF]

, 2018
Actinobacillus pleuropneumoniae (A. pleuropneumoniae) is a Gram-negative bacterium that represents the main cause of porcine pleuropneumonia in pigs, causing significant economic losses to the livestock industry worldwide. A.
A Hensel, A Kulp, A Maas, A Menzel, Alannah Deeney, Anders Miki Bojesen, Andrew Rycroft, B Kim, BS Collins, Cathrine Ørskov, Cyrielle Fougeroux, D Hoeltig, D Reimer, DJ Chen, E Negrete-Abascal, E Negrete-Abascal, F Antenucci, F Xie, Fabio Antenucci, FM Aarestrup, G Vernikos, H Bosch van den, H Huang, H Huang, H Sanders, I Overbeke Van, J Frey, J Frey, JL Jobert, JQ Tumamao, JT Bossé, JT Bossé, K Chiers, K Chiers, K Klitgaard, L Pol van der, L Sadilkova, M Hagberg, M Pritsch, M Ramjeet, M Shao, M Torremorell, M Vanni, MJ Jacobsen, NL Price, OG González, PC Hannan, Peter Johannes Holst, R Acevedo, R Sarkozi, S Thrane, Sacristán R Pozo Del, SE Pors, WC Losinger, X Xie, Y Zhou   +55 more
core   +6 more sources

Structural analysis of the Actinobacillus pleuropneumoniae-RTX-toxin I (ApxI) operon [PDF]

Infection and Immunity, 1993
Actinobacillus pleuropneumoniae-RTX-toxin I (ApxI), an important virulence factor, is secreted by serotypes 1, 5, 9, 10, and 11 of A. pleuropneumoniae. However, sequences homologous to the secretion genes apxIBD of the ApxI operon are present in all 12 serotypes except serotype 3. The purpose of this study was to determine and compare the structures of
R, Jansen, J, Briaire, E M, Kamp, A L, Gielkens, M A, Smits   +4 more
openaire   +2 more sources

Distinct Roles of the Repeat-Containing Regions and Effector Domains of the Vibrio vulnificus Multifunctional-Autoprocessing Repeats-in-Toxin (MARTX) Toxin

mBio, 2015
Vibrio vulnificus is a seafood-borne pathogen that destroys the intestinal epithelium, leading to rapid bacterial dissemination and death. The most important virulence factor is the multifunctional-autoprocessing repeats-in-toxin (MARTX) toxin comprised ...
Byoung Sik Kim, Hannah E. Gavin, Karla J. F. Satchell   +2 more
doaj   +1 more source

Peptide-based ligand antagonists block a Vibrio cholerae adhesin. [PDF]

FEBS Lett
The structure of a peptide‐binding domain of the Vibrio cholerae adhesin FrhA was solved by X‐ray crystallography, revealing how the inhibitory peptide AGYTD binds tightly at its Ca2+‐coordinated pocket. Structure‐guided design incorporating D‐amino acids enhanced binding affinity, providing a foundation for developing anti‐adhesion therapeutics ...
Wang M, Du G, Yongo-Luwawa C, Lu A, Kinrade B, Munro K, Klose KE, Lubell WD, Davies P, Guo S.   +9 more
europepmc   +2 more sources

Interdomain Contacts and the Stability of Serralysin Protease from Serratia marcescens. [PDF]

PLoS ONE, 2015
The serralysin family of bacterial metalloproteases is associated with virulence in multiple modes of infection. These extracellular proteases are members of the Repeats-in-ToXin (RTX) family of toxins and virulence factors, which mediated virulence in E.
Liang Zhang, Anneliese J Morrison, Patrick H Thibodeau   +2 more
doaj   +1 more source

Role of peptidergic nerve terminals in the skin: reversal of thermal sensation by calcitonin gene-related peptide in TRPV1-depleted neuropathy. [PDF]

PLoS ONE, 2012
To investigate the contribution of peptidergic intraepidermal nerve fibers (IENFs) to nociceptive responses after depletion of the thermal-sensitive receptor, transient receptor potential vanilloid subtype 1 (TRPV1), we took advantage of a ...
Yu-Lin Hsieh, Chih-Lung Lin, Hao Chiang, Yaw-Syan Fu, June-Horng Lue, Sung-Tsang Hsieh   +5 more
doaj   +1 more source

Abundant toxin-related genes in the genomes of beneficial symbionts from deep-sea hydrothermal vent mussels [PDF]

, 2015
Bathymodiolus mussels live in symbiosis with intracellular sulfur-oxidizing (SOX) bacteria that provide them with nutrition. We sequenced the SOX symbiont genomes from two Bathymodiolus species.
Achaz, Altschul, Anantharaman, Backert, Badger, Bailly, Bateman, Benz, Bettencourt, Bhavsar, Boeckmann, Bradford, Brinkhoff, Buchan, Caspi, Cavanaugh, Cavanaugh, Chambers, Christie-Oleza, Clayton, Cossart, Coustau, da Silva, Dale, Dale, Davies, Davis, De Wit, DeChaine, Degnan, Delcher, Distel, Dmytrenko, Dobrindt, Douglas, Dubilier, Duperron, Duperron, Duperron, Elias, Emanuelsson, Eng, Eymann, Finn, Fisher, Florens, Fontanez, Galagan, Gardebrecht, Gebruk, Goffredi, Gogarten, Goodrich-Blair, Haglund, Halary, Harada, Harmer, Hart, Heinz, Hentschel, Hopkins, Hueck, Hunter, Jackson, Jiggins, Kadar, Kaebernick, Kanehisa, Katoh, Kearse, Kelley, Kleiner, Kleiner, Kobayashi, Koskiniemi, Krogh, Kung, Kuwahara, Kwak, Käll, Lagesen, Langmead, Lauenstein, Lavik, Li, Lindsay, Linhartová, Liu, Liu, Lowe, Ludwig, Ma, Markert, Markert, Markowitz, McClure, McFall-Ngai, McKenna, Melvin, Meusch, Meyer, Minguez, Moebius, Moreira, Murillo, Muyzer, Newton, Newton, Ochman, Ogier, Ohno, Oliver, Oliver, Oliver, Paerl, Parks, Partida-Martinez, Pernthaler, Petersen, Petersen, Petersen, Petersen, Ponting, Poole, Powell, Pruesse, Quast, Quinlan, R Development Core Team, Rasko, Reams, Richter, Riou, Rissman, Robidart, Rocha, Roig, Ronquist, Rouchet, Russell, Sakiyama, Sakiyama, Sarrazin, Satchell, Satchell, Schmid, Shannon, Snyder, Soucy, Srinivasan, Stamatakis, Steele-Mortimer, Strous, Sunamura, Takeuchi, Tatusov, Van Dover, Van Dover, Vogl, von Cosel, Wagner-Döbler, Walsh, Ward, Wardle, Waterfield, Wentrup, West, Wittkop, Won, Won, Wood, Wright, Zhang, Zhou, Zielinski, Zuleta   +175 more
core   +2 more sources