Results 51 to 60 of about 2,957 (188)

Thymol Protects Channel Catfish from Aeromonas hydrophila Infection by Inhibiting Aerolysin Expression and Biofilm Formation

Microorganisms, 2020
Aeromonas hydrophila is an opportunistic pathogen responsible for a number of diseases in freshwater farming. Moreover, the bacterium has been identified as a zoonotic pathogen that threatens human health.
Jing Dong, Lushan Zhang, Yongtao Liu, Ning Xu, Shun Zhou, Qiuhong Yang, Yibin Yang, Xiaohui Ai   +7 more
doaj   +1 more source

Electrophoresis and Electroosmosis in Aerolysin and Hemolysin Nanopores [PDF]

Biophysical Journal, 2016
Voltage-dependent interaction of macromolecules with biological nanopores can arise from electroosmotic (EOF) or electrophoretic (EPF) forces. Both poly(ethylene-glycol) (PEG), and cyclodextrins (β- and α-CD, respectively) block the ionic current through α-hemolysin (αHL) and Aerolysin (AeL) pore-forming proteins with well-documented voltage-dependence.
Boukhet, Mordjane, Pelta, Juan, Behrends, Jan C., Oukhaled, Abdelghani   +3 more
openaire   +1 more source

Crossing three membranes Channel formation by aerolysin [PDF]

FEBS Letters, 1992
Aerolysin is a channel‐forming toxin responsible for the pathogenicity of Aeromonas hydrophila. It crosses the inner and outer membranes of the bacteria in separate steps and is released as a 52‐kDa inactive protoxin which is activated by proteolytic removal of approximately 40 amino acids from the C terminus.
openaire   +2 more sources

Activation of the hole-forming toxin aerolysin by extracellular processing [PDF]

Journal of Bacteriology, 1985
A precursor-product relationship between aerolysin and a protein with a higher molecular weight was observed in culture supernatants of Aeromonas hydrophila. The larger protein was isolated by ammonium sulfate precipitation and ion-exchange and hydroxyapatite chromatography and compared with purified aerolysin.
S P, Howard, J T, Buckley
openaire   +2 more sources

Aerolysin imaging.

, 2014
Aerolysin variants, fluorescently labeled, bind to the cell surface of HeLa cells. Images were acquired by confocal fluorescence microscopy. A Single labeled aerolysin versions.
Irene Wuethrich (268882), Carla P. Guimaraes (638509), Christopher S. Theile (638507), Hidde L. Ploegh (32525), Eric Spooner (155228), Annet E. M. Blom (638506), Janneke G. C. Peeters (525403), Zeyang Li (638508)   +7 more
core   +1 more source

Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

Nature Communications, 2016
Lysenin is member of the aerolysin family of small ß-barrel pore-forming toxins that include virulence factors from several human and animal pathogens. Here the authors determine the structure of the lysenin pore by single particle cryo- EM and propose a
Monika Bokori-Brown, Thomas G. Martin, Claire E. Naylor, Ajit K. Basak, Richard W. Titball, Christos G. Savva   +5 more
doaj   +1 more source

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism [PDF]

, 2013
Aerolysin is the founding member of a superfamily of β-pore-forming toxins whose pore structure is unknown. We have combined X-ray crystallography, cryo-EM, molecular dynamics and computational modeling to determine the structures of aerolysin mutants in
Ioan Iacovache, Matteo Dal Peraro, Dal Peraro, Matteo, Degiacomi, M., Dal Peraro, M., van der Goot, F., Kudryashev, M., Lacovache, Ioan, F Gisou van der Goot, Kudryashev, Misha, van der Goot, F Gisou, Pernot, L., Degiacomi, Matteo T., Stahlberg, Henning, Iacovache, Ioan, Kudryashev, M. ; https://orcid.org/, Iacovache, I., Matteo T Degiacomi, Lucile Pernot, van der Goot, F.G., Chami, Mohamed, van der Goot, F. Gisou, Chami, M., Stahlberg, H., Pernot, Lucile, Degiacomi, M.T., Mohamed Chami, Misha Kudryashev, Henning Stahlberg   +28 more
core   +1 more source

Methanol extract of Black soldier fly (Hermetia illucens) prepupae against Aeromonas and Staphylococcus aureus bacteria in vitro and in silico

Open Veterinary Journal, 2023
Background: Staphylococcus and Aeromonas bacteria are pathogens in humans and animals. The therapy disrupts the virulence structure of the bacteria, resulting in bacterial death.
Dahliatul Qosimah, Sanarto Santosa, Maftuch Maftuch, Husnul Khotimah, Loeki Enggar Fitri, Aulanni'am Aulanni'am, Lucia Tri Suwanti   +6 more
doaj   +1 more source

Aerolysin induces G-protein activation and Ca2+ release from intracellular stores in human granulocytes

, 1998
Aerolysin is a pore-forming toxin that plays a key role in the pathogenesis of Aeromonas hydrophila infections. In this study, we have analyzed the effect of aerolysin on human granulocytes (HL-60 cells).
van der Goot, F. G., Fivaz, M., Krause, Karl-Heinz, Monod, Antoinette   +3 more
core   +2 more sources

Study of some cytogenetic effects of Aerolysin Produced by Aeromonas hydrophila on normal and tumor cells in vitro.

مجلة مركز بحوث التقنيات الاحيائية, 2010
This study aimed to find the cytotoxicity of the aerolysin produced by Aeromonas hydrophila on rat embryo fibroblast, mouse mammary adeno carcinoma and human larynx epidermal carcinoma cell lines by estimating the cells inhibitory and proliferation ...
Sanaa Jassem Al- Baidani, Abdul Hussain Moyet Al-Faisal, Norrya A. Ali   +2 more
doaj   +1 more source