Rodriguez H

References (7)

Title : A structurally unique Fusobacterium nucleatum tannase provides detoxicant activity against gallotannins and pathogen resistance - Mancheno_2022_Microb.Biotechnol_15_648
Author(s) : Mancheno JM , Atondo E , Tomas-Cortazar J , Luis Lavin J , Plaza-Vinuesa L , Martin-Ruiz I , Barriales D , Palacios A , Daniel Navo C , Sampedro L , Pena-Cearra A , Angel Pascual-Itoiz M , Castelo J , Carreras-Gonzalez A , Castellana D , Pellon A , Delgado S , Ruas-Madiedo P , de Las Rivas B , Abecia L , Munoz R , Jimenez-Oses G , Anguita J , Rodriguez H
Ref : Microb Biotechnol , 15 :648 , 2022
Abstract : Colorectal cancer pathogenesis and progression is associated with the presence of Fusobacterium nucleatum and the reduction of acetylated derivatives of spermidine, as well as dietary components such as tannin-rich foods. We show that a new tannase orthologue of F. nucleatum (TanBF(nn) ) has significant structural differences with its Lactobacillus plantarum counterpart affecting the flap covering the active site and the accessibility of substrates. Crystallographic and molecular dynamics analysis revealed binding of polyamines to a small cavity that connects the active site with the bulk solvent which interact with catalytically indispensable residues. As a result, spermidine and its derivatives, particularly N(8) -acetylated spermidine, inhibit the hydrolytic activity of TanBF(nn) and increase the toxicity of gallotannins to F. nucleatum. Our results support a model in which the balance between the detoxicant activity of TanBF(nn) and the presence of metabolic inhibitors can dictate either conducive or unfavourable conditions for the survival of F. nucleatum.
ESTHER : Mancheno_2022_Microb.Biotechnol_15_648
PubMedSearch : Mancheno_2022_Microb.Biotechnol_15_648
PubMedID: 33336898
Gene_locus related to this paper: fusnn-FN0616

Title : Bacterial tannases: classification and biochemical properties - de Las Rivas_2019_Appl.Microbiol.Biotechnol_103_603
Author(s) : de Las Rivas B , Rodriguez H , Anguita J , Munoz R
Ref : Applied Microbiology & Biotechnology , 103 :603 , 2019
Abstract : Tannin acyl hydrolases, also known as tannases, are a group of enzymes critical for the transformation of tannins. The study of these enzymes, which initially evolved in different organisms to detoxify and/or use these plant metabolites, has nowadays become relevant in microbial enzymology research due to their relevant role in food tannin transformation. Microorganisms, particularly bacteria, are major sources of tannase. Cloning and heterologous expression of bacterial tannase genes and structural studies have been performed in the last few years. However, a systematic compilation of the information related to all recombinant tannases, their classification, and characteristics is missing. In this review, we explore the diversity of heterologously produced bacterial tannases, describing their substrate specificity and biochemical characterization. Moreover, a new classification based on sequence similarity analysis is proposed. Finally, putative tannases have been identified in silico for each group of tannases taking advantage of the use of the "tannase" distinctive features previously proposed.
ESTHER : de Las Rivas_2019_Appl.Microbiol.Biotechnol_103_603
PubMedSearch : de Las Rivas_2019_Appl.Microbiol.Biotechnol_103_603
PubMedID: 30460533

Title : Identification of a highly active tannase enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum - Tomas-Cortazar_2018_Microb.Cell.Fact_17_33
Author(s) : Tomas-Cortazar J , Plaza-Vinuesa L , de Las Rivas B , Lavin JL , Barriales D , Abecia L , Mancheno JM , Aransay AM , Munoz R , Anguita J , Rodriguez H
Ref : Microb Cell Fact , 17 :33 , 2018
Abstract : BACKGROUND: Tannases are tannin-degrading enzymes that have been described in fungi and bacteria as an adaptative mechanism to overcome the stress conditions associated with the presence of these phenolic compounds. RESULTS: We have identified and expressed in E. coli a tannase from the oral microbiota member Fusobacterium nucleatum subs. polymorphum (TanBFnp). TanBFnp is the first tannase identified in an oral pathogen. Sequence analyses revealed that it is closely related to other bacterial tannases. The enzyme exhibits biochemical properties that make it an interesting target for industrial use. TanBFnp has one of the highest specific activities of all bacterial tannases described to date and shows optimal biochemical properties such as a high thermal stability: the enzyme keeps 100% of its activity after prolonged incubations at different temperatures up to 45 degrees C. TanBFnp also shows a wide temperature range of activity, maintaining above 80% of its maximum activity between 22 and 55 degrees C. The use of a panel of 27 esters of phenolic acids demonstrated activity of TanBFnp only against esters of gallic and protocatechuic acid, including tannic acid, gallocatechin gallate and epigallocatechin gallate. Overall, TanBFnp possesses biochemical properties that make the enzyme potentially useful in biotechnological applications. CONCLUSIONS: We have identified and characterized a metabolic enzyme from the oral pathogen Fusobacterium nucleatum subsp. polymorphum. The biochemical properties of TanBFnp suggest that it has a major role in the breakdown of complex food tannins during oral processing. Our results also provide some clues regarding its possible participation on bacterial survival in the oral cavity. Furthermore, the characteristics of this enzyme make it of potential interest for industrial use.
ESTHER : Tomas-Cortazar_2018_Microb.Cell.Fact_17_33
PubMedSearch : Tomas-Cortazar_2018_Microb.Cell.Fact_17_33
PubMedID: 29482557
Gene_locus related to this paper: fusnp-a5txs5

Title : A comparative evaluation of biological activities and bioactive compounds of the seagrasses Zostera marina and Zostera noltei from southern Portugal - Custodio_2016_Nat.Prod.Res_30_724
Author(s) : Custodio L , Laukaityte S , Engelen AH , Rodrigues MJ , Pereira H , Vizetto-Duarte C , Barreira L , Rodriguez H , Albericio F , Varela J
Ref : Nat Prod Res , 30 :724 , 2016
Abstract : This work assessed the antioxidant potential, acetylcholinesterase (AChE) inhibition and the in vitro cytotoxic activity of extracts of the seagrasses Zostera marina and Zostera noltei collected from southern Portugal. The total phenolic contents (TPCs), the rosmarinic acid (RA) concentration (HPLC/DAD) and the fatty acid (FA) profile (GC/MS) are also described. Z. marina had the highest TPC, radical scavenging activity against DPPH radicals and copper chelating activity. Z. noltei had metal chelation capacity to copper and iron ions. None of the species was able to inhibit AChE. Both seagrasses had high levels of polyunsaturated FAs. Z. marina significantly and selectively reduced the viability of tumorous neuronal cells. Z. noltei was highly toxic for the three cell lines tested and was selective against hepatocarcinoma cells at the concentration of 100 mug/mL. RA was the main compound identified in Z. marina, but not in Z. noltei.
ESTHER : Custodio_2016_Nat.Prod.Res_30_724
PubMedSearch : Custodio_2016_Nat.Prod.Res_30_724
PubMedID: 26189828

Title : The genome of a pathogenic rhodococcus: cooptive virulence underpinned by key gene acquisitions - Letek_2010_PLoS.Genet_6_e1001145
Author(s) : Letek M , Gonzalez P , Macarthur I , Rodriguez H , Freeman TC , Valero-Rello A , Blanco M , Buckley T , Cherevach I , Fahey R , Hapeshi A , Holdstock J , Leadon D , Navas J , Ocampo A , Quail MA , Sanders M , Scortti MM , Prescott JF , Fogarty U , Meijer WG , Parkhill J , Bentley SD , Vazquez-Boland JA
Ref : PLoS Genet , 6 :e1001145 , 2010
Abstract : We report the genome of the facultative intracellular parasite Rhodococcus equi, the only animal pathogen within the biotechnologically important actinobacterial genus Rhodococcus. The 5.0-Mb R. equi 103S genome is significantly smaller than those of environmental rhodococci. This is due to genome expansion in nonpathogenic species, via a linear gain of paralogous genes and an accelerated genetic flux, rather than reductive evolution in R. equi. The 103S genome lacks the extensive catabolic and secondary metabolic complement of environmental rhodococci, and it displays unique adaptations for host colonization and competition in the short-chain fatty acid-rich intestine and manure of herbivores--two main R. equi reservoirs. Except for a few horizontally acquired (HGT) pathogenicity loci, including a cytoadhesive pilus determinant (rpl) and the virulence plasmid vap pathogenicity island (PAI) required for intramacrophage survival, most of the potential virulence-associated genes identified in R. equi are conserved in environmental rhodococci or have homologs in nonpathogenic Actinobacteria. This suggests a mechanism of virulence evolution based on the cooption of existing core actinobacterial traits, triggered by key host niche-adaptive HGT events. We tested this hypothesis by investigating R. equi virulence plasmid-chromosome crosstalk, by global transcription profiling and expression network analysis. Two chromosomal genes conserved in environmental rhodococci, encoding putative chorismate mutase and anthranilate synthase enzymes involved in aromatic amino acid biosynthesis, were strongly coregulated with vap PAI virulence genes and required for optimal proliferation in macrophages. The regulatory integration of chromosomal metabolic genes under the control of the HGT-acquired plasmid PAI is thus an important element in the cooptive virulence of R. equi.
ESTHER : Letek_2010_PLoS.Genet_6_e1001145
PubMedSearch : Letek_2010_PLoS.Genet_6_e1001145
PubMedID: 20941392
Gene_locus related to this paper: coreq-e9sxw6 , coreq-e9t5k8 , coreq-e9t5k9 , coreq-e9t7v9 , rhoha-e9t397 , rhoe1-e4w8b9 , rhoe1-e4w8k3 , rhoe1-e4w8s0 , rhoe1-e4w9r2 , rhoe1-e4wah6 , rhoe1-e4wb26 , rhoe1-e4wb75 , rhoe1-e4wdz9 , rhoe1-e4wg39 , rhoe1-e4wg83 , rhoe1-e4whm4 , rhoe1-e4wih4 , rhoe1-e4wja5 , rhoe1-e4wjd9 , rhoe1-e4wjy2 , rhoe1-e4wat8 , coreq-e9t814 , rhoe1-e4wbp9 , coreq-e9t0s6 , coreq-e9swc5 , rhoe1-e4wix8 , rhoe1-e4wjy1

Title : Production and physicochemical properties of recombinant Lactobacillus plantarum tannase - Curiel_2009_J.Agric.Food.Chem_57_6224
Author(s) : Curiel JA , Rodriguez H , Acebron I , Mancheno JM , de Las Rivas B , Munoz R
Ref : Journal of Agricultural and Food Chemistry , 57 :6224 , 2009
Abstract : Tannase is an enzyme with important biotechnological applications in the food industry. Previous studies have identified the tannase encoding gene in Lactobacillus plantarum and also have reported the description of the purification of recombinant L. plantarum tannase through a protocol involving several chromatographic steps. Here, we describe the high-yield production of pure recombinant tannase (17 mg/L) by a one-step affinity procedure. The purified recombinant tannase exhibits optimal activity at pH 7 and 40 degrees C. Addition of Ca(2+) to the reaction mixture greatly increased tannase activity. The enzymatic activity of tannase was assayed against 18 simple phenolic acid esters. Only esters derived from gallic acid and protocatechuic acid were hydrolyzed. In addition, tannase activity was also assayed against the tannins tannic acid, gallocatechin gallate, and epigallocatechin gallate. Despite L. plantarum tannase representing a novel family of tannases, which shows no significant similarity to tannases from fungal sources, both families of enzymes shared similar substrate specificity range. The physicochemical characteristics exhibited by L. plantarum recombinant tannase make it an adequate alternative to the currently used fungal tannases.
ESTHER : Curiel_2009_J.Agric.Food.Chem_57_6224
PubMedSearch : Curiel_2009_J.Agric.Food.Chem_57_6224
PubMedID: 19601665
Gene_locus related to this paper: lacpl-tanL

Title : Characterization of tannase activity in cell-free extracts of Lactobacillus plantarum CECT 748T - Rodriguez_2008_Int.J.Food.Microbiol_121_92
Author(s) : Rodriguez H , de Las Rivas B , Gomez-Cordoves C , Munoz R
Ref : Int J Food Microbiol , 121 :92 , 2008
Abstract : In foods, tannins are considered nutritionally undesirable. Spectrophotometric methods have been used to detect tannin degradation by L. plantarum strains isolated from food substrates. Enzymatic degradation of tannic acid by L. plantarum CECT 748T was examined in liquid cultures and in cell-free extracts by HPLC. Significative reduction of tannic acid was not observed during incubation in the presence of L. plantarum cells after 7 days incubation. However, tannic acid was effectively degraded by cell-free extracts of L. plantarum during 16 h incubation. We have partially characterized L. plantarum tannase activity by measuring its esterase activity on methyl gallate. Tannase activity was optimal at pH 5.0 and 30 degrees C, and showed nearly 75% of the maximal activity at 50 degrees C. The biochemical characteristics showed by L. plantarum tannase are considered favourable for tannin biodegradation in the food-processing industry.
ESTHER : Rodriguez_2008_Int.J.Food.Microbiol_121_92
PubMedSearch : Rodriguez_2008_Int.J.Food.Microbiol_121_92
PubMedID: 18054106