نتایج جستجو برای: cholera toxin subunit b

تعداد نتایج: 1022123  

Journal: :Infection and immunity 2003
Song F Lee Scott A Halperin Danny F Salloum Ann MacMillan Annette Morris

A chimeric protein consisting of a divalent pertussis toxin (PT) S1 fragment linked to the cholera toxin (Ctx) A(2)B fragment was constructed. The chimera induced a mucosal immunoglobulin A (IgA) and a serum IgG immune response to PT and CtxB in BALB/c mice following intranasal immunization. The immune sera neutralized PT in vitro. In the mouse model of Bordetella pertussis respiratory infectio...

Journal: :Infection and immunity 1991
Y Lobet C W Cluff W Cieplak

Previous studies of the S1 subunit of pertussis toxin, an NAD(+)-dependent ADP-ribosyltransferase, suggested that a small amino-terminal region of amino acid sequence similarity to the active fragments of both cholera toxin and Escherichia coli heat-labile enterotoxin represents a region containing critical active-site residues that might be involved in the binding of the substrate NAD+. Other ...

Journal: :Journal of Neuroscience Methods 2021

Retrograde and anterograde transsynaptic viral vectors are useful tools for studying the input output organization of neuronal circuitry, respectively. While retrograde widely used, that show transduction not common. We chose recombinant avian adeno-associated virus (A3V) carrying mCherry gene injected it into eyeball, cochlear duct, midbrain auditory center chickens. observed different surviva...

Journal: :Biophysical journal 2006
Jonathan P Williams Daniel C Smith Brian N Green Brian D Marsden Keith R Jennings Lynne M Roberts James H Scrivens

Cholera toxin (CTx) is an AB5 cytotonic protein that has medical relevance in cholera and as a novel mucosal adjuvant. Here, we report an analysis of the noncovalent homopentameric complex of CTx B chain (CTx B5) using electrospray ionization triple quadrupole mass spectrometry and tandem mass spectrometry and the analysis of the noncovalent hexameric holotoxin usingelectrospray ionization time...

Journal: :The American journal of physiology 1998
Florencia B Schapiro Clifford Lingwood Wendy Furuya Sergio Grinstein

A small fraction of the molecules internalized by endocytosis reaches the Golgi complex through a retrograde pathway that is poorly understood. In the present work, we used bacterial toxins to study the retrograde pathway in Vero cells. The recombinant B subunit of verotoxin 1B (VT1B) was labeled with fluorescein to monitor its progress within the cell by confocal microscopy. This toxin, which ...

2012
Kazuhisa Okada Amonrattana Roobthaisong Ichiro Nakagawa Shigeyuki Hamada Siriporn Chantaroj

BACKGROUND Vibrio cholerae O1 El Tor dominated the seventh cholera pandemic which occurred in the 1960s. For two decades, variants of V. cholerae O1 El Tor that produce classical cholera toxin have emerged and spread globally, replacing the prototypic El Tor biotype. This study aims to characterize V. cholerae O1 isolates from outbreaks in Thailand with special reference to genotypic variations...

2015
Ka Lok Hong Eamonn Maher Ryan M Williams Letha J Sooter

Toxin B is one of the major virulence factors of Clostridium difficile, a bacterium that is responsible for a significant number of diarrhea cases in acute care settings. Due to the prevalence of C. difficile induced diarrhea, rapid and correct diagnosis is crucial in the disease management. In this study, we have employed a stringent in vitro selection method to identify single-stranded DNA mo...

2013
Srikar Reddy Michael Taylor Mojun Zhao Patrick Cherubin Sandra Geden Supriyo Ray David Francis Ken Teter

Vibrio cholerae produces cholera toxin (CT), an AB5 protein toxin that is primarily responsible for the profuse watery diarrhea of cholera. CT is secreted into the extracellular milieu, but the toxin attacks its Gsα target within the cytosol of a host cell. Thus, CT must cross a cellular membrane barrier in order to function. This event only occurs after the toxin travels by retrograde vesicula...

Journal: :The Biochemical journal 1993
T M Schepers K R McLeish

N-Formylmethionyl-leucyl-phenylalanine (fMet-Leu-Phe) and leukotriene B4 (LTB4) induce disparate second-messenger generation and functional responses in neutrophils and HL-60 granulocytes. Receptors for these chemoattractants couple to a common pool of G-proteins which are substrates for both pertussis-toxin- and cholera-toxin-catalysed ADP-ribosylation. The hypothesis that formyl-peptide and L...

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