Association of tannase-producing Staphylococcus lugdunensis with colon cancer and characterization of a novel tannase gene

Noguchi, Norihisa; Ohashi, Takashi; Shiratori, Taisei; Narui, Koji; Hagiwara, Tadashi; Ko, Mari; Watanabe, Kiyoshi; Miyahara, Takeo; Taira, Satoru; Moriyasu, Fuminori; Sasatsu, Masanori

doi:10.1007/s00535-007-2012-5

Cited by 70 publications

(46 citation statements)

References 34 publications

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“…Indeed, a gene, tanA, encoding a 596-aa-long protein 43% identical to the tannase recently described for Staphylococcus lugdunensis (46), is present in its genome. Like S. lugdunensis tannase, TanA is predicted to be exported and contains a conserved lipobox motif (LTACS) at the cleavage site of the signal peptide, indicating that it may be a lipoprotein that remains attached to the cell membrane.…”

Section: Resultsmentioning

confidence: 99%

Genome Sequence ofStreptococcus gallolyticus: Insights into Its Adaptation to the Bovine Rumen and Its Ability To Cause Endocarditis

et al. 2010

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Streptococcus gallolyticus (formerly known as Streptococcus bovis biotype I) is an increasing cause of endocarditis among streptococci and frequently associated with colon cancer. S. gallolyticus is part of the rumen flora but also a cause of disease in ruminants as well as in birds. Here we report the complete nucleotide sequence of strain UCN34, responsible for endocarditis in a patient also suffering from colon cancer. Analysis of the 2,239 proteins encoded by its 2,350-kb-long genome revealed unique features among streptococci, probably related to its adaptation to the rumen environment and its capacity to cause endocarditis. S. gallolyticus has the capacity to use a broad range of carbohydrates of plant origin, in particular to degrade polysaccharides derived from the plant cell wall. Its genome encodes a large repertoire of transporters and catalytic activities, like tannase, phenolic compounds decarboxylase, and bile salt hydrolase, that should contribute to the detoxification of the gut environment. Furthermore, S. gallolyticus synthesizes all 20 amino acids and more vitamins than any other sequenced Streptococcus species. Many of the genes encoding these specific functions were likely acquired by lateral gene transfer from other bacterial species present in the rumen. The surface properties of strain UCN34 may also contribute to its virulence. A polysaccharide capsule might be implicated in resistance to innate immunity defenses, and glucan mucopolysaccharides, three types of pili, and collagen binding proteins may play a role in adhesion to tissues in the course of endocarditis.

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Section: Resultsmentioning

confidence: 99%

Genome Sequence ofStreptococcus gallolyticus: Insights into Its Adaptation to the Bovine Rumen and Its Ability To Cause Endocarditis

et al. 2010

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“…Despite the extensive interest and long history of the study of tannase, there is surprisingly little knowledge about the enzyme at the molecular level, which has become one of the critical factors that limit the large-scale application of tannase. To our knowledge, the only bacterial tannases that have been analyzed genetically are those from Staphylococcus lugdunensis (6), Lactobacillus plantarum (7,8), and Enterobacter sp. (9).…”

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confidence: 99%

Tannin Degradation by a Novel Tannase Enzyme Present in Some Lactobacillus plantarum Strains

Jiménez

Esteban-Torres

Mancheño

et al. 2014

Appl Environ Microbiol

109

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bLactobacillus plantarum is frequently isolated from the fermentation of plant material where tannins are abundant. L. plantarum strains possess tannase activity to degrade plant tannins. An L. plantarum tannase (TanB Lp , formerly called TanLp1) was previously identified and biochemically characterized. In this study, we report the identification and characterization of a novel tannase (TanA Lp ). While all 29 L. plantarum strains analyzed in the study possess the tanB Lp gene, the gene tanA Lp was present in only four strains. Upon methyl gallate exposure, the expression of tanB Lp was induced, whereas tanA Lp expression was not affected. TanA Lp showed only 27% sequence identity to TanB Lp , but the residues involved in tannase activity are conserved. Optimum activity for TanA Lp was observed at 30°C and pH 6 in the presence of Ca 2؉ ions. TanA Lp was able to hydrolyze gallate and protocatechuate esters with a short aliphatic alcohol substituent. Moreover, TanA Lp was able to fully hydrolyze complex gallotannins, such as tannic acid. The presence of the extracellular TanA Lp tannase in some L. plantarum strains provides them an advantage for the initial degradation of complex tannins present in plant environments.

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“…Detannification of foods and feeds by applying tannase can improve their palatability, digestibility and nutritive value (4,2). Tannase is used in removing haze from tea beverages (5), tea cream solubilization (6) and as a biomarker for colon cancer (7). It is also used in agricultural waste and tannin polluting industrial effluents treatment (8,9).…”

Section: Introductionmentioning

confidence: 99%

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2017

RJLBPCS

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Tannase (Tannin acyl hydrolase, EC 3.1.1.20), an industrially important enzyme, is predominantly produced by bacteria as well as fungi. Present study reports evolutionary relatedness among 112 fungal tannase protein sequences through superfamily/family search and protein sequences based phylogenetic analysis. Although all the selected tannase sequences belonged to alpha/beta-Hydrolase superfamily, but they were distributed in different families. Most of the Auricularia were related to Haloperoxidase family but maximum Aspergillus sp. showed relation with Hypothetical protein TT16620 family. This differentiation was also observed in phylogenetic analysis where Auricularia sp. and Stereum sp.were found in one cluster and Aspergillus sp. in another cluster thus indicating prominent sequence divergency.Comparison among whole protein and domain based phylogeny revealed gradual separation of related species in different blocks followed by species specific functional tannase motif identification. A total of 85 sequences were found with six common blocks among which block 2 and 4 showed relation with tannase function. Again motif 1 of block 2 (KTYWNGCSTGGREGMKQVQRF) and motif 1 of block 4 (FQERGGKMIHYHGEAD PCIPTANSVHYWQ) also showed tannase function, which could be used for species specific probe designing on PCR amplification. Subcellular localization of fungal tannase protein sequences revealed that most of the sequences were secretory in nature. Localization study will disclose the metabolic network of fungal tannase associated with mitochondria and other organelle too. Sequence and structure based analysis of Auricularia delicata (Acc. No. EJD47898.1) and Aspergillus kawachii (Acc. No. GAA89804.1) tannase protein indicated structures are more conserved than sequences and the diversity occurs at loop positions.Banerjee et al RJLBPCS 2017

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Association of tannase-producing Staphylococcus lugdunensis with colon cancer and characterization of a novel tannase gene

Abstract: Tannase-producing S. lugdunensis is associated with advanced-stage colon cancer, and the tanA gene is a useful marker for the detection of S. lugdunensis.

Cited by 70 publications

References 34 publications

Genome Sequence ofStreptococcus gallolyticus: Insights into Its Adaptation to the Bovine Rumen and Its Ability To Cause Endocarditis

Genome Sequence ofStreptococcus gallolyticus: Insights into Its Adaptation to the Bovine Rumen and Its Ability To Cause Endocarditis

Tannin Degradation by a Novel Tannase Enzyme Present in Some Lactobacillus plantarum Strains

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