Regulation of pertussis toxin and lipopolysaccharide levels of Bordetella pertussis 134 in response to modulators
Authors
Abstract:
Whooping cough (pertussis) is a highly contagious disease of the human respiratory tract, which is caused by Bordetella pertussis. Reemerge of pertussis in some highly immunized populations and divergency in gene order among several B. pertussis strains promoted this research to study the change of pertussis toxin (PT) and lipopolysacharide levels in response to the different environments. This study conducted an extensive investigation of antigenic modulation of B. pertussis strain 134 in the presence of different chemicals. One of the findings of this research, for the first time, was that barium ion has growth inhibitory role on B. pertussis 134, when added in high concentration to CBA plates. Nicotinic acid, magnesium sulfate, and magnesium chloride have shown the significant modulating effect on the basis of reduction of PT levels. Our data demonstrated quantitatively that the modulation of B. pertussis yields high levels of LPS. Our results have showed the strong modulatory effects of FeCl3 on reduction of PT levels. In general, this study provided collective data which are strongly applicable to explain modulation of B. pertussis, and also introduces new modulators which promote more study on gene order of B. pertussis.
similar resources
regulation of pertussis toxin and lipopolysaccharide levels of bordetella pertussis 134 in response to modulators
whooping cough (pertussis) is a highly contagious disease of the human respiratory tract, which is caused by bordetella pertussis. reemerge of pertussis in some highly immunized populations and divergency in gene order among several b. pertussis strains promoted this research to study the change of pertussis toxin (pt) and lipopolysacharide levels in response to the different environments. this...
full textPertussis toxin and lipopolysaccharide influence phagocytosis of Bordetella pertussis by human monocytes.
The potential of human monocytes to mediate the clearance of Bordetella pertussis infection was examined. Bacteria expressing green fluorescent protein were incubated with adherent peripheral blood monocytes, and phagocytosis was quantified by using fluorescence microscopy. Monocytes internalized only a small percentage of the adherent bacteria. Surface-associated Bvg-regulated virulence factor...
full textAnalysis of relative levels of production of pertussis toxin subunits and Ptl proteins in Bordetella pertussis.
Pertussis toxin is transported across the outer membrane of Bordetella pertussis by the type IV secretion system known as the Ptl transporter, which is composed of nine different proteins. In order to determine the relative levels of production of pertussis toxin subunits and Ptl proteins in B. pertussis, we constructed translational fusions of the gene for alkaline phosphatase, phoA, with vari...
full textPertussis Toxin Stimulates IL-17 Production in Response to Bordetella pertussis Infection in Mice
In a mouse model of respiratory tract infection by Bordetella pertussis, bacteria multiply in the airways over the first week and are then cleared over the next 3-4 weeks by the host immune response. Pertussis toxin (PT), a virulence factor secreted exclusively by B. pertussis, promotes bacterial growth in the airways by suppression and modulation of host immune responses. By comparison of wild...
full textBordetella pertussis Strain Lacking Pertactin and Pertussis Toxin.
A Bordetella pertussis strain lacking 2 acellular vaccine immunogens, pertussis toxin and pertactin, was isolated from an unvaccinated infant in New York State in 2013. Comparison with a French strain that was pertussis toxin-deficient, pertactin wild-type showed that the strains carry the same 28-kb deletion in similar genomes.
full textMembrane localization of the S1 subunit of pertussis toxin in Bordetella pertussis and implications for pertussis toxin secretion.
Pertussis toxin is secreted from Bordetella pertussis with the assistance of the Ptl transport system, a member of the type IV family of macromolecular transporters. The S1 subunit and the B oligomer combine to form the holotoxin prior to export from the bacterial cell, although the site of assembly is not known. To better understand the pathway of pertussis toxin assembly and secretion, we exa...
full textMy Resources
Journal title
volume 62 issue 3
pages 135- 144
publication date 2007-09-01
By following a journal you will be notified via email when a new issue of this journal is published.
Hosted on Doprax cloud platform doprax.com
copyright © 2015-2023