Demonstration of epithelium-associated microbes in the oesophagus of pigs, cattle, rats and deer

Tannock, Gerald W.; Blumershine, Ruth V. H.; Archibald, Rae W.

doi:10.1111/j.1574-6968.1987.tb02356.x

Cited by 25 publications

(15 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lactobacillus, one of the common indigenous organisms of the gastrointestinal tracts of mammals (46,48,49) and a potential probiotic microbe that contributes to the health of the host (11,16), has the capacity to adhere to epithelial cells (5,6,9,10,16,21,23,24,33,34,44,49) and mucus gel (25,32,35,38,41,51,52) from the intestinal tracts of different species. Lactobacillus surface proteins have been proposed to be involved in colonization of gastrointestinal epithelial cells and mucosa of mammals (9,12,21,41,44,53).…”

mentioning

confidence: 99%

Purification and Characterization of a Surface Protein from Lactobacillus fermentum 104R That Binds to Porcine Small Intestinal Mucus and Gastric Mucin

Rojas-Contreras

Ascencio²,

Conway

2002

Appl Environ Microbiol

161

124

View full text Add to dashboard Cite

An adhesion-promoting protein involved in the binding of Lactobacillus fermentum strain 104R to small intestinal mucus from piglets and to partially purified gastric mucin was isolated and characterized. Spent culture supernatant fluid and bacterial cell wall extracts were fractionated by ammonium sulfate precipitation and gel filtration. The active fraction was purified by affinity chromatography. The adhesion-promoting protein was detected in the fractions by adhesion inhibition and dot blot assays and visualized by polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate-PAGE, and Western blotting with horseradish peroxidaselabeled mucus and mucin. The active fraction was characterized by estimating the relative molecular weight and by assessing the presence of carbohydrates in, and heat sensitivity of, the active region of the adhesionpromoting protein. The purified protein was digested with porcine trypsin, and the peptides were purified in a SMART system. The peptides were tested for adhesion to horseradish peroxidase-labeled mucin by using the dot blot adhesion assay. Peptides which bound mucin were sequenced. It was shown that the purified adhesionpromoting protein on the cell surface of L. fermentum 104R is extractable with 1 M LiCl and low concentrations of lysozyme but not with 0.2 M glycine. The protein could be released to the culture supernatant fluid after 24 h of growth and had affinity for both small intestinal mucus and gastric mucin. In the native state this protein was variable in size, and it had a molecular mass of 29 kDa when denatured. The denatured protein did not contain carbohydrate moieties and was not heat sensitive. Alignment of amino acids of the adhering peptides with sequences deposited in the EMBL data library showed poor homology with previously published sequences. The protein represents an important molecule for development of probiotics.Proteinaceous surface appendages or coverings, e.g., fimbriae, flagella, or surface (S)-layers with affinity for mammalian extracellular matrix (55) or mucosa (17, 28), have been extensively characterized for many pathogenic bacteria. It is thought that adhesion to mammalian extracellular matrix components is a prerequisite for bacterial colonization and invasion to subepithelial tissues (55) Cell surface-adhesive proteins from nonpathogenic bacteria and their role in colonization has not been as thoroughly characterized.Lactobacillus, one of the common indigenous organisms of the gastrointestinal tracts of mammals (46,48,49) and a potential probiotic microbe that contributes to the health of the host (11,16), has the capacity to adhere to epithelial cells (5,6,9,10,16,21,23,24,33,34,44,49) and mucus gel (25,32,35,38,41,51,52) from the intestinal tracts of different species. Lactobacillus surface proteins have been proposed to be involved in colonization of gastrointestinal epithelial cells and mucosa of mammals (9,12,21,41,44,53). Collagen binding by lactobacilli (1, 47) is known, and purification of collagen binding proteins from L...

show abstract

mentioning

confidence: 99%

Purification and Characterization of a Surface Protein from Lactobacillus fermentum 104R That Binds to Porcine Small Intestinal Mucus and Gastric Mucin

Rojas-Contreras

Ascencio²,

Conway

2002

Appl Environ Microbiol

161

124

View full text Add to dashboard Cite

show abstract

“…It has been strongly suggested that lactobacilli can colonize the non-secretory epithelium of the stomach by attachment to epithelial cells, and continuously inoculate gastric contents and the lower regions of the intestinal tract (Fuller et ril. 1978;Tannock et al 1987). Less attention has been diverted towards colonization of secreting mucosa by by lactobacilli and the mechanism of adhesion to immobilized mucus, has recently been studied (Henriksson 1993).…”

Section: Introductionmentioning

confidence: 98%

“…Many studies have focused on the mechanism of attachment to epithelial cells from the pars oesophageal region of non-secreting keratinized epithelium (Suegara rt al. 1975;Lin and Savage 1984;Tannock et al 1987;Henriksson rt al. 1991).…”

Section: Introductionmentioning

confidence: 98%

Colonization by lactobacilli of piglet small intestinal mucus

Rojas-Contreras

Conway

1996

Journal of Applied Bacteriology

View full text Add to dashboard Cite

The colonization potential of lactobacilli was investigated using small intestinal mucus extracts from 35-d-old pigs. Mucus-secreting tissue from the small intestine of piglets was gently rinsed to remove contents and then shaken in buffer to release mucus from the surface. Numbers of lactobacilli in different portions of the small intestine of 35-d-old pigs were enumerated. Also, mucus isolated from the small intestine of pigs was investigated for its capacity to support the growth of lactobacilli. Results indicated that Lactobacillus spp. inhabit the mucus layer of the small intestine and can grow and adhere to ileal mucus. From adhesion studies of Lactobacillus fermentum 104R to mucus analysed by Scatchard plot, it is suggested that an associating system showing positive cooperativity is involved. Proteinaceous compounds(s) involved in the adhesion to mucus were detected in the spent culture fluid from the growth of strain 104R. Studies are continuing in order to identify and characterize the adhesion-promoting protein(s). From the data, it is proposed that lactobacilli colonize the mucus layer of the small intestine of pigs.

show abstract

“…Currently, Lactobacillus is a probiotic commonly supplemented to human and animal diets for maintaining the intestinal ecosystem and integrity. Lactobacilli are major indigenous inhabitants in the GIT, and some select species have been used extensively as probiotic cultures [1][2][3][4]. Lactobacillus can survive intestinal transit [5] and exert beneficial effects in vivo, which can modify the digestive microflora, maintain the intestinal ecosystem, and stimulate the immune system during their passage through the digestive tract [6,7].…”

Section: Introductionmentioning

confidence: 99%

2‐DE and MS analysis of interactions between Lactobacillus fermentum I5007 and intestinal epithelial cells

Yang

Wang

et al. 2007

Electrophoresis

View full text Add to dashboard Cite

Lactobacillus is a probiotic commonly used for supplementation to human and animal diets. In this study, we used 2-DE and MS to analyze changes in the proteomes of Lactobacillus and intestinal epithelial cells in two model systems. The in vivo and in vitro models were involved the inoculation of Lactobacillus fermentum I5007 into the rabbit jejunum for 4 h and the culture of the bacterium with Caco-2 cells for 1 h, respectively. Our results indicate that, after exposure to the intestinal environment, the bacterium exhibited decreases in key enzymes involved in energy metabolism (e.g., lactate dehydrogenase, dihydrolipoamide dehydrogenase, and nicotinate phosphoribosyltransferase) and amino acid metabolism (e.g., arginyl-tRNA synthetase and aspartate-semialdehyde dehydrogenase), but increases in glycoside hydrolase (an enzyme for mucin degradation) and fructose-6-phosphate phosphoketolase (an enzyme of the pentose phosphate pathway). In response to an interaction with L. fermentum I5007, Caco-2 cells showed changes in proteins that were beneficial for gut integrity, including voltage-dependent anion channel 1, glutathione transferase, and heat shock protein gp96. On the basis of their functions, we suggest that these proteins serve as useful biomarkers for metabolic changes in Lactobacillus and intestinal epithelial cells in response to their interactions.

show abstract

Demonstration of epithelium-associated microbes in the oesophagus of pigs, cattle, rats and deer

Abstract: Scanning electron microscope or light microscope examination of oesphageal specimens demonstrated the association of microbial cells with the epithelial surface. Rod‐shaped bacteria and cocci were seen in specimens obtained from pigs and rats, cocci in specimens from cattle, and rods

Cited by 25 publications

References 8 publications

Purification and Characterization of a Surface Protein from Lactobacillus fermentum 104R That Binds to Porcine Small Intestinal Mucus and Gastric Mucin

Purification and Characterization of a Surface Protein from Lactobacillus fermentum 104R That Binds to Porcine Small Intestinal Mucus and Gastric Mucin

Colonization by lactobacilli of piglet small intestinal mucus

2‐DE and MS analysis of interactions between Lactobacillus fermentum I5007 and intestinal epithelial cells

Contact Info

Product

Resources

About