ArticleVirulence2015
Characterization of an α-l-fucosidase from the periodontal pathogen Tannerella forsythia.
Article in Virulence, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- Structural elucidation and characterization of GH29A α-l-fucosidases and the effect of pH on their transglycosylation.The FEBS journal · 2025Article
- Microbiological and molecular aspects of periodontitis pathogenesis: an infection-induced inflammatory condition.Frontiers in cellular and infection microbiology · 2025Review
- Mechanisms of recalcitrant fucoidan breakdown in marine Planctomycetota.Nature communications · 2024Article
- A Robust α-l-Fucosidase fromACS chemical biology · 2024Article
- Exploring the sequence-function space of microbial fucosidases.Communications chemistry · 2024Article
- α-L-Fucosidases from an Alpaca Faeces Metagenome: Characterisation of Hydrolytic and Transfucosylation Potential.International journal of molecular sciences · 2024Article
- Identification and Characterization of a Novel α-L-Fucosidase fromInternational journal of molecular sciences · 2023Article
- Structure and function of microbial α-l-fucosidases: a mini review.Essays in biochemistry · 2023Review
- Multispecies biofilm behavior and host interaction support the association of Tannerella serpentiformis with periodontal health.Molecular oral microbiology · 2023Article
- A Combination of Structural, Genetic, Phenotypic and Enzymatic Analyses Reveals the Importance of a Predicted Fucosyltransferase to ProteinBiomolecules · 2021Article
- The dental plaque biofilm matrix.Periodontology 2000 · 2021Review
- Fucosidases from the human gut symbiont Ruminococcus gnavus.Cellular and molecular life sciences : CMLS · 2021Article
- Comparative genome characterization of the periodontal pathogen Tannerella forsythia.BMC genomics · 2020Article
- Nonulosonic acids contribute to the pathogenicity of the oral bacteriumInterface focus · 2019Review
- Tannerella forsythia strains display different cell-surface nonulosonic acids: biosynthetic pathway characterization and first insight into biological implications.Glycobiology · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Outer membrane vesicles of Tannerella forsythia: biogenesis, composition, and virulence.Molecular oral microbiology · 2015Article
- Oral infections: clinical and biological perspectives.Virulence · 2015Article
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
The periodontal pathogen Tannerella forsythia expresses several glycosidases which are linked to specific growth requirements and are involved in the invasion of host tissues. α-l-Fucosyl residues are exposed on various host glycoconjugates and, thus, the α-l-fucosidases predicted in the T. forsythia ATCC 43037 genome could potentially serve roles in host-pathogen interactions. We describe the molecular cloning and characterization of the putative fucosidase TfFuc1 (encoded by the bfo_2737 = Tffuc1 gene), previously reported to be present in an outer membrane preparation. In terms of sequence, this 51-kDa protein is a member of the glycosyl hydrolase family GH29. Using an artificial substrate, p-nitrophenyl-α-fucose (KM 670 μM), the enzyme was determined to have a pH optimum of 9.0 and to be competitively inhibited by fucose and deoxyfuconojirimycin. TfFuc1 was shown here to be a unique α(1,2)-fucosidase that also possesses α(1,6) specificity on small unbranched substrates. It is active on mucin after sialidase-catalyzed removal of terminal sialic acid residues and also removes fucose from blood group H. Following knock-out of the Tffuc1 gene and analyzing biofilm formation and cell invasion/adhesion of the mutant in comparison to the wild-type, it is most likely that the enzyme does not act extracellularly. Biochemically interesting as the first fucosidase in T. forsythia to be characterized, the biological role of TfFuc1 may well be in the metabolism of short oligosaccharides in the periplasm, thereby indirectly contributing to the virulence of this organism. TfFuc1 is the first glycosyl hydrolase in the GH29 family reported to be a specific α(1,2)-fucosidase.
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