A structurally unique Fusobacterium nucleatum tannase provides detoxicant activity against gallotannins and pathogen resistance

Abstract

A new tannase enzyme from the cancer‐related pathogen Fusobacterium nucleatum is important for the survival of the bacteria under the stress conditions derived from the presence of dietary gallotannins. Using structural studies and molecular modelling we describe new structural features for this enzyme. The inhibition of the enzyme by spermidine and its acetylated derivatives conduce to higher susceptibility to diet phenolic gallotannins and decreased fitness of F. nucleatum.

Structural diversity and substrate preferences of three tannase enzymes encoded by the anaerobic bacterium Clostridium butyricum

“…The overall structure adopted the α/β hydrolase fold (6 α-helices and 8 β-sheets) with multiple inserts that formed an additional 12 helices and 5 β-sheets (Fig. S7), which is similar to the additional inserts observed in other crystallized bacterial tannases (22,30). Chain A and B could be built from residues 1-490, with a single chain break in chain A and two in chain B. Residues from 116-135 (between β5 and α2, Fig.…”

Biochemical and Structural Characterization of a Novel Bacterial Tannase From Lachnospiraceae bacterium in Ruminant Gastrointestinal Tract

“…nucleatum (GenBank Accession No. ALQ42581.1) ( Mancheño et al, 2020 ) and 40.4% with TanASl from Staphylococcus lugdunensis (GenBank Accession No. BAF03594.1) ( Rusniok et al, 2010 ).…”

“…On the basis of these results, we can conclude that TanA Lb has high substrate affinity and catalytic efficiency for depside bonds. In addition, TanA Lb is capable of degrading not only esters of phenolic acid with short chain aliphatic alcohols but also esters of phenolic acids with long chain alcohols such as lauryl gallate, similar to TanB Fnp and TanB Fnn ( Tomás-Cortázar et al, 2018 ; Mancheño et al, 2020 ).…”

“…In agreement with the sequence alignment, the structural characterization, therefore, indicated that TanA Lb belongs to the α / β -hydrolase superfamily ( Remington et al, 1992 ). It is worth noting that the TanA Lb contained an insertion of a 109 residue stretch (residues 341–450) ( Figure 4B ), which is the largest structural deviation and may assume the role of the flap covering the active site of the enzyme ( Mancheño et al, 2020 ).…”

“…The optimum temperature and pH value for biochemical characteristics of bacterial tannases are 30°C–50°C and 3.0–7.0, respectively ( Lekshmi et al, 2021 ). Up to now, two kinds of bacterial tannase belonging to probiotics (TanA Lp , Lactobacillus plantarum ) and the oral bacteria (TanB Fnn , Fusobacterium nucleatum ) have been structurally characterized by combining crystal structure, molecular dynamics, and mutation analysis, which confirmed the functional role of the flap domain and flap-like domain in the substrate recognition and specificity of tannase ( Ren et al, 2013 ; Mancheño et al, 2020 ).…”