scholarly journals Autoinducer-2 Production in Campylobacter jejuni Contributes to Chicken Colonization

2008 ◽  
Vol 75 (1) ◽  
pp. 281-285 ◽  
Author(s):  
Beatriz Qui�ones ◽  
William G. Miller ◽  
Anna H. Bates ◽  
Robert E. Mandrell
Keyword(s):  
Gastrointestinal Tract ◽  
Epithelial Cells ◽  
Organic Acids ◽  
Campylobacter Jejuni ◽  
Hepatoma Cells ◽  
Lower Gastrointestinal Tract ◽  
Host Colonization ◽  
Autoinducer 2

ABSTRACT Inactivation of luxS, encoding an AI-2 biosynthesis enzyme, in Campylobacter jejuni strain 81-176 significantly reduced colonization of the chick lower gastrointestinal tract, chemotaxis toward organic acids, and in vitro adherence to LMH chicken hepatoma cells. Thus, AI-2 production in C. jejuni contributes to host colonization and interactions with epithelial cells.

scholarly journals A σ28-Regulated Nonflagella Gene Contributes to Virulence of Campylobacter jejuni 81-176

2006 ◽  
Vol 74 (1) ◽  
pp. 769-772 ◽  
Author(s):  
Scarlett Goon ◽  
Cheryl P. Ewing ◽  
Maria Lorenzo ◽  
Dawn Pattarini ◽  
Gary Majam ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Campylobacter Jejuni ◽  
Diarrheal Disease ◽  
Intestinal Epithelial Cells ◽  
Disease Model ◽  
Intestinal Epithelial ◽  
Model Expression

ABSTRACT A Campylobacter jejuni 81-176 mutant in Cj0977 was fully motile but reduced >3 logs compared to the parent in invasion of intestinal epithelial cells in vitro. The mutant was also attenuated in a ferret diarrheal disease model. Expression of Cj0977 protein was dependent on a minimal flagella structure.

scholarly journals Role of Campylobacter jejuni Respiratory Oxidases and Reductases in Host Colonization

2008 ◽  
Vol 74 (5) ◽  
pp. 1367-1375 ◽  
Author(s):  
Rebecca A. Weingarten ◽  
Jesse L. Grimes ◽  
Jonathan W. Olson
Keyword(s):  
Campylobacter Jejuni ◽  
Anaerobic Respiration ◽  
Wild Type ◽  
Respiratory Enzymes ◽  
Host Colonization ◽  
Enzymatic Function ◽  
Food Borne ◽  
Transport Chain ◽  
Respiratory Oxidases

ABSTRACT Campylobacter jejuni is the leading cause of human food-borne bacterial gastroenteritis. The C. jejuni genome sequence predicts a branched electron transport chain capable of utilizing multiple electron acceptors. Mutants were constructed by disrupting the coding regions of the respiratory enzymes nitrate reductase (napA::Cm), nitrite reductase (nrfA::Cm), dimethyl sulfoxide, and trimethylamine N-oxide reductase (termed Cj0264::Cm) and the two terminal oxidases, a cyanide-insensitive oxidase (cydA::Cm) and cbb3-type oxidase (ccoN::Cm). Each strain was characterized for the loss of the associated enzymatic function in vitro. The strains were then inoculated into 1-week-old chicks, and the cecal contents were assayed for the presence of C. jejuni 2 weeks postinoculation. cydA::Cm and Cj0264c::Cm strains colonized as well as the wild type; napA::Cm and nrfA::Cm strains colonized at levels significantly lower than the wild type. The ccoN::Cm strain was unable to colonize the chicken; no colonies were recovered at the end of the experiment. While there appears to be a role for anaerobic respiration in host colonization, oxygen is the most important respiratory acceptor for C. jejuni in the chicken cecum.

scholarly journals In vitro study on the effect of organic acids on Campylobacter jejuni/coli populations in mixtures of water and feed

2002 ◽  
Vol 81 (5) ◽  
pp. 621-628 ◽  
Author(s):  
P Chaveerach ◽  
D.A. Keuzenkamp ◽  
H.A. Urlings ◽  
L.J. Lipman ◽  
F van Knapen
Keyword(s):  
Organic Acids ◽  
Campylobacter Jejuni ◽  
In Vitro Study ◽  
Vitro Study

In Vitro Effects of Thymol-β-d-Glucopyranoside on Salmonella enterica Serovar Typhimurium and Escherichia coli K88†

2016 ◽  
Vol 79 (2) ◽  
pp. 299-303 ◽  
Author(s):  
G. LEVENT ◽  
R. B. HARVEY ◽  
G. CIFTCIOGLU ◽  
R. C. BEIER ◽  
K. J. GENOVESE ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Gastrointestinal Tract ◽  
Pure Culture ◽  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Lower Gastrointestinal Tract ◽  
Serovar Typhimurium ◽  
In Vitro Effects ◽  
Porcine Feces

ABSTRACT Although thymol is bactericidal against many pathogens in vitro, its in vivo effectiveness against pathogens in the lower gastrointestinal tract is limited because of its rapid absorption in the proximal gut. Thymol-β-d-glucopyranoside (β-thymol), a conjugated form of thymol, can deliver thymol to the lower gastrointestinal tract and has shown antibacterial effects. In the present study, we examined the in vitro effects of β-thymol on Salmonella enterica serovar Typhimurium (ST) and Escherichia coli K88 (K88). We inoculated one-half strength Mueller-Hinton broth with 5.8 ± 0.09 log CFU/ml novobiocin- and naladixic acid–resistant (NN) ST (NVSL 95-1776) and 5.1 ± 0.09 log CFU ml−1 NN-resistant K88, with or without porcine feces (0.1% [wt/vol]) (fecal incubations). The resultant bacterial suspensions were distributed under N2 to triplicate sets of tubes to achieve initial concentrations of 0, 3, 6, and 12 mM for ST treatments and 0, 3, 12, and 30 mM for K88 treatments. Samples were incubated at 39°C and then plated onto NN-containing brilliant green agar and NN-containing MacConkey agar; ST and K88 CFU concentrations were determined via 10-fold dilutions, and viable cell counts were performed at 0, 6, and 24 h. No differences in ST CFU counts were observed in β-thymol–treated tubes without the added porcine feces (i.e., pure culture) at 6 or 24 h. However, in tubes that contained fecal incubations, ST CFU counts were reduced (P < 0.05) from controls at 6 h in tubes treated with 6 and 12 mM β-thymol, whereas in tubes treated with 3, 6, and 12 mM β-thymol the CFU counts were reduced (P < 0.05) at 24 h. No differences were observed in K88 CFU counts in pure culture or in fecal incubations at 6 h, but K88 CFU counts were reduced (P < 0.05) in both pure and fecal incubations at 24 h. The results from this study demonstrate that β-thymol, in the presence of fecal suspensions, has anti-Salmonella and anti–E. coli effects, suggesting a role of β-glycoside–hydrolyzing microbes for the release of bactericidal thymol from β-thymol.

scholarly journals Examination of Campylobacter jejuni Putative Adhesins Leads to the Identification of a New Protein, Designated FlpA, Required for Chicken Colonization

2009 ◽  
Vol 77 (6) ◽  
pp. 2399-2407 ◽  
Author(s):  
Rebecca C. Flanagan ◽  
Jason M. Neal-McKinney ◽  
A. Singh Dhillon ◽  
William G. Miller ◽  
Michael E. Konkel
Keyword(s):  
Epithelial Cells ◽  
Campylobacter Jejuni ◽  
Blot Hybridization ◽  
Broiler Chicks ◽  
Cell Adherence ◽  
Dot Blot ◽  
Dot Blot Hybridization ◽  
Genes Encoding

ABSTRACT Campylobacter jejuni colonization of chickens is presumably dependent upon multiple surface-exposed proteins termed adhesins. Putative C. jejuni adhesins include CadF, CapA, JlpA, major outer membrane protein, PEB1, Cj1279c, and Cj1349c. We examined the genetic relatedness of 97 C. jejuni isolates recovered from human, poultry, bovine, porcine, ovine, and canine sources by multilocus sequence typing (MLST) and examined their profile of putative adhesin-encoding genes by dot blot hybridization. To assess the individual contribution of each protein in bacterium-host cell adherence, the C. jejuni genes encoding the putative adhesins were disrupted by insertional mutagenesis. The phenotype of each mutant was judged by performing in vitro cell adherence assays with chicken LMH hepatocellular carcinoma epithelial cells and in vivo colonization assays with broiler chicks. MLST analysis indicated that the C. jejuni isolates utilized in this study were genetically diverse. Dot blot hybridization revealed that the C. jejuni genes encoding the putative adhesins, with the exception of capA, were conserved among the isolates. The C. jejuni CadF, CapA, Cj1279c, and Cj1349c proteins were found to play a significant role in the bacterium's in vitro adherence to chicken epithelial cells, while CadF, PEB1, and Cj1279c were determined to play a significant role in the bacterium's in vivo colonization of broiler chicks. Collectively, the data indicate that Cj1279c is a novel adhesin. Because Cj1279c harbors fibronectin type III domains, we designated the protein FlpA, for fibronectin-like protein A.

scholarly journals Polyphosphate kinases modulate Campylobacter jejuni outer membrane constituents and alter its capacity to invade and survive in intestinal epithelial cells in vitro

2015 ◽  
Vol 4 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Ruby Pina-Mimbela ◽  
Jesús Arcos Madrid ◽  
Anand Kumar ◽  
Jordi B Torrelles ◽  
Gireesh Rajashekara
Keyword(s):  
Epithelial Cells ◽  
Outer Membrane ◽  
Campylobacter Jejuni ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial

scholarly journals Effect of extruding on ruminal disappearance and lower gastrointestinal tract digestion of white lupin seeds

1993 ◽  
Vol 73 (3) ◽  
pp. 571-579 ◽  
Author(s):  
A. R. Kibelolaud ◽  
M. Vernay ◽  
C. Bayourthe ◽  
R. Moncoulon
Keyword(s):  
Gastrointestinal Tract ◽  
Crude Protein ◽  
Lupinus Albus ◽  
Neutral Detergent Fiber ◽  
White Lupin ◽  
Lower Gastrointestinal Tract ◽  
Rumen Degradation ◽  
Outflow Rate ◽  
Lupin Seeds

The effect of extruding white lupin (Lupinus albus 'Lublanc') seeds (WLS) at 110, 130, 150 or 180 °C on the in vitro solubility of crude protein (CP) and in sacco rumen degradation and intestinal digestion of rumen escape CP and fiber was determined. Rumen degradation was estimated by incubating nylon bags in the rumen of cows for 2, 4, 8, 16, 24 and 48 h. Extruding WLS at 110, 130, 150 and 180 °C reduced the CP-solubility by 32.8, 47.7, 58.4 and 67.5%, respectively. The effective ruminal degradabilities of CP, acid detergent fiber (ADF) and neutral detergent fiber (NDF) were evaluated assuming a ruminal outflow rate of 0.06 h−1. Heating WLS at 110, 130, 150 and 180 °C decreased the ruminal degradability of CP value: 89.8, 79.9, 65.1, 61.8 vs. 93.4% (raw), respectively; the corresponding values for ADF and NDF were: 38.4, 35.3, 34.2, 27.6 vs. 43.6% (raw) and 37.7, 33.1, 32.2, 26.5 vs. 39.4% (raw). Postruminal digestion was estimated using a sequence of ruminal in situ incubation for 4, 8 and 16 h, in vitro incubation in an acid-pepsin bath for 3 h and a mobile nylon bag technique distal to the abomasum. Extrusion of WLS decreased the degradability of CP, ADF and NDF in the rumen with a corresponding increase in the amounts digested in the postruminal sections; the whole-tract digestibility was generally unchanged. Therefore, the processing shifted the digestion of these components from rumen to the lower gastrointestinal tract. Key words: White lupin seed, in vitro solubility, rumen degradability, postruminal digestion, crude protein, detergent fiber

scholarly journals The Dual-Functioning Fumarate Reductase Is the Sole Succinate:Quinone Reductase in Campylobacter jejuni and Is Required for Full Host Colonization

2009 ◽  
Vol 191 (16) ◽  
pp. 5293-5300 ◽  
Author(s):  
Rebecca A. Weingarten ◽  
Michael E. Taveirne ◽  
Jonathan W. Olson
Keyword(s):  
Organic Acids ◽  
Succinate Dehydrogenase ◽  
Campylobacter Jejuni ◽  
Growth Phase ◽  
Tca Cycle ◽  
Fumarate Reductase ◽  
Wild Type ◽  
Succinate Dehydrogenase Activity

ABSTRACT Campylobacter jejuni encodes all the enzymes necessary for a complete oxidative tricarboxylic acid (TCA) cycle. Because of its inability to utilize glucose, C. jejuni relies exclusively on amino acids as the source of reduced carbon, and they are incorporated into central carbon metabolism. The oxidation of succinate to fumarate is a key step in the oxidative TCA cycle. C. jejuni encodes enzymes annotated as a fumarate reductase (Cj0408 to Cj0410) and a succinate dehydrogenase (Cj0437 to Cj0439). Null alleles in the genes encoding each enzyme were constructed. Both enzymes contributed to the total fumarate reductase activity in vitro. The frdA::cat + strain was completely deficient in succinate dehydrogenase activity in vitro and was unable to perform whole-cell succinate-dependent respiration. The sdhA::cat + strain exhibited wild-type levels of succinate dehydrogenase activity both in vivo and in vitro. These data indicate that Frd is the only succinate dehydrogenase in C. jejuni and that the protein annotated as a succinate dehydrogenase has been misannotated. The frdA::cat + strain was also unable to grow with the characteristic wild-type biphasic growth pattern and exhibited only the first growth phase, which is marked by the consumption of aspartate, serine, and associated organic acids. Substrates consumed in the second growth phase (glutamate, proline, and associated organic acids) were not catabolized by the the frdA::cat + strain, indicating that the oxidation of succinate is a crucial step in metabolism of these substrates. Chicken colonization trials confirmed the in vivo importance of succinate oxidation, as the frdA::cat + strain colonized chickens at significantly lower levels than the wild type, while the sdhA::cat + strain colonized chickens at wild-type levels.

Sign in / Sign up

Export Citation Format

Share Document