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Research Paper

Characterization of an α-l-fucosidase from the periodontal pathogen Tannerella forsythia

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Pages 282-292 | Received 05 Dec 2014, Accepted 16 Jan 2015, Published online: 15 Apr 2015

References

  • Vos T, Flaxman AD, Naghavi M, Lozano R, Michaud C, Ezzati M, Shibuya K, Salomon JA, Abdalla S, Aboyans V., et al. Years lived with disability (YLDs) for 1160 sequelae of 289 diseases and injuries 1990-2010: a systematic analysis for the global burden of disease study 2010. Lancet 2012; 380:2163-96; PMID:23245607; http://dx.doi.org/10.1016/S0140-6736(12)61729-2
  • Socransky SS, Haffajee AD, Cugini MA, Smith C, Kent RL Jr. Microbial complexes in subgingival plaque. J Clin Periodontol 1998; 25:134-44; PMID:9495612; http://dx.doi.org/10.1111/j.1600-051X.1998.tb02419.x
  • Haffajee AD, Socransky SS, Patel MR, Song X. Microbial complexes in supragingival plaque. Oral Microbiol Immunol 2008; 23:196-205; PMID:18402605; http://dx.doi.org/10.1111/j.1399-302X.2007.00411.x
  • Cullinan MP, Ford PJ, Seymour GJ. Periodontal disease and systemic health: current status. Aust Dent J 2009; 54:S62-9; PMID:19737269; http://dx.doi.org/10.1111/j.1834-7819.2009.01144.x
  • Posch G, Sekot G, Friedrich V, Megson ZA, Koerdt A, Messner P, Schäffer C. Glycobiology aspects of the periodontal pathogen tannerella forsythia. Biomolecules 2012; 2:467-82; PMID:24970146; http://dx.doi.org/10.3390/biom2040467
  • Sekot G, Posch G, Oh YJ, Zayni S, Mayer HF, Pum D, Messner P, Hinterdorfer P, Schäffer C. Analysis of the cell surface layer ultrastructure of the oral pathogen tannerella forsythia. Arch Microbiol 2012; 194:525-39; PMID:22273979; http://dx.doi.org/10.1007/s00203-012-0792-3
  • Lee SW, Sabet M, Um HS, Yang J, Kim HC, Zhu W. Identification and characterization of the genes encoding a unique surface (S-) layer of tannerella forsythia. Gene 2006; 371:102-11; PMID:16488557; http://dx.doi.org/10.1016/j.gene.2005.11.027
  • Posch G, Pabst M, Brecker L, Altmann F, Messner P, Schäffer C. Characterization and scope of S-layer protein O-glycosylation in tannerella forsythia. J Biol Chem 2011; 286:38714-24; PMID:21911490; http://dx.doi.org/10.1074/jbc.M111.284893
  • Sabet M, Lee SW, Nauman RK, Sims T, Um HS. The surface (S-) layer is a virulence factor of bacteroides forsythus. Microbiol 2003; 149:3617-27; PMID:14663093; http://dx.doi.org/10.1099/mic.0.26535-0
  • Sakakibara J, Nagano K, Murakami Y, Higuchi N, Nakamura H, Shimozato K, Yoshimura F. Loss of adherence ability to human gingival epithelial cells in S-layer protein-deficient mutants of tannerella forsythensis. Microbiol 2007; 153:866-76; PMID:17322207; http://dx.doi.org/10.1099/mic.0.29275-0
  • Honma K, Inagaki S, Okuda K, Kuramitsu HK, Sharma A. Role of a tannerella forsythia exopolysaccharide synthesis operon in biofilm development. Microb Pathog 2007; 42:156-66; PMID:17363213; http://dx.doi.org/10.1016/j.micpath.2007.01.003
  • Douglas CO, Naylor K, Phansopa C, Frey AM, Farmilo T, Stafford GP. Physiological adaptations of key oral bacteria. Adv Microb Physiol 2014; 65:257-335; PMID:25476768; http://dx.doi.org/10.1002/mbo3.233
  • Stafford G, Roy S, Honma K, Sharma A. Sialic acid, periodontal pathogens and Tannerella forsythia: stick around and enjoy the feast! Mol Oral Microbiol 2012; 27:11-22; PMID:22230462; http://dx.doi.org/10.1111/j.2041-1014.2011.00630.x
  • Honma K, Mishima E, Sharma A. Role of tannerella forsythia NanH sialidase in epithelial cell attachment. Infect Immun 2011; 79:393-401; PMID:21078857; http://dx.doi.org/10.1128/IAI.00629-10
  • Roy S, Honma K, Douglas CW, Sharma A, Stafford GP. Role of sialidase in glycoprotein utilization by tannerella forsythia. Microbiol 2011; 157:31953-202; PMID:21885482; http://dx.doi.org/10.1099/mic.0.052498-0
  • Duran-Pinedo AE, Chen T, Teles R, Starr JR, Wang X, Krishnan K, Frias-Lopez J. Community-wide transcriptome of the oral microbiome in subjects with and without periodontitis. ISME J 2014; 8:1659-72; PMID:24599074; http://dx.doi.org/10.1038/ismej.2014.23
  • Lühn K, Wild MK. Human deficiencies of fucosylation and sialylation affecting selectin ligands. Semin Immunopathol 2012; 34:383-99; PMID:22461019; http://dx.doi.org/10.1007/s00281-012-0304-1
  • Bode L, Jantscher-Krenn E. Structure-function relationships of human milk oligosaccharides. Adv Nutr 2012; 3:383S-91S; PMID:22585916; http://dx.doi.org/10.3945/an.111.001404
  • Katayama T, Sakuma A, Kimura T, Makimura Y, Hiratake J, Sakata K, Yamanoi T, Kumagai H, Yamamoto K. Molecular cloning and characterization of bifidobacterium bifidum 1,2-α-L-fucosidase (AfcA), a novel inverting glycosidase (glycoside hydrolase family 95). J Bacteriol 2004; 186:4885-93; PMID:15262925; http://dx.doi.org/10.1128/JB.186.15.4885-4893.2004
  • Boren T, Falk P, Roth KA, Larson G, Normark S. Attachment of helicobacter pylori to human gastric epithelium mediated by blood group antigens. Science 1993; 262:1892-5; PMID:8018146; http://dx.doi.org/10.1126/science.8018146
  • Ruiz-Palacios GM, Cervantes LE, Ramos P, Chavez-Munguia B, Newburg DS. Campylobacter jejuni binds intestinal H(O) antigen (fuca1, 2Gal b1, 4GlcNAc), and fucosyloligosaccharides of human milk inhibit its binding and infection. J Biol Chem 2003; 278:14112-20; PMID:12562767; http://dx.doi.org/10.1074/jbc.M207744200
  • Stahl M, Friis LM, Nothaft H, Liu X, Li J, Szymanski CM, intzi A. L-fucose utilization provides campylobacter jejuni with a competitive advantage. Proc Natl Acad Sci U S A 2011; 108:7194-9; PMID:21482772; http://dx.doi.org/10.1073/pnas.1014125108
  • Coyne MJ, Reinap B, Lee MM, Comstock LE. Human symbionts use a host-like pathway for surface fucosylation. Science 2005; 307:1778-81; PMID:15774760; http://dx.doi.org/10.1126/science.1106469
  • Veith PD, O'Brien-Simpson NM, Tan Y, Djatmiko DC, Dashper SG, Reynolds EC. Outer membrane proteome and antigens of tannerella forsythia. J Proteome Res 2009; 8:4279-92; PMID:19663511; http://dx.doi.org/10.1021/pr900372c
  • Guillotin L, Lafite P, Daniellou R. Unraveling the substrate recognition mechanism and specificity of the unusual glycosyl hydrolase family 29 BT2192 from bacteroides thetaiotaomicron. Biochem 2014; 53:1447-55; PMID:24527659; http://dx.doi.org/10.1021/bi400951q
  • Berteau O, McCort I, Goasdoué N, Tissot B, Daniel R. Characterization of a new α-L-fucosidase isolated from the marine mollusk Pecten maximus that catalyzes the hydrolysis of α-L-fucose from algal fucoidan (ascophyllum nodosum). Glycobiol 2002; 12:273-82; PMID:12042250; http://dx.doi.org/10.1093/glycob/12.4.273
  • Rodríguez-Diaz J, Monedero V, Yebra MJ. Utilization of natural fucosylated oligosaccharides by three novel α-L-fucosidases from a probiotic lactobacillus casei strain. Appl Environ Microbiol 2011; 77:703-5; PMID:21097595; http://dx.doi.org/10.1128/AEM.01906-10
  • Winchester B, Barker C, Baines S, Jacob GS, Namgoong SK, Fleet G. Inhibition of α-L-fucosidase by derivatives of deoxyfuconojirimycin and deoxymannojirimycin. Biochem J 1990; 265:277-82; PMID:2137330
  • Hajishengallis G, Lamont RJ. Beyond the red complex and into more complexity: the polymicrobial synergy and dysbiosis (PSD) model of periodontal disease etiology. Mol Oral Microbiol 2012; 27:409-19; PMID:23134607; http://dx.doi.org/10.1111/j.2041-1014.2012.00663.x
  • Marsh PD. Are dental diseases examples of ecological catastrophes? Microbiol 2003; 149:279-94; PMID:12624191; http://dx.doi.org/10.1099/mic.0.26082-0
  • Marsh PD, Moter A, Devine DA. Dental plaque biofilms: communities, conflict and control. Periodontol 2000 2011; 55:16-35; PMID:21134226; http://dx.doi.org/10.1111/j.1600-0757.2009.00339.x
  • Tomek MB, Neumann L, Nimeth I, Koerdt A, Andesner P, Messner P, Mach L, Potempa JS, Schäffer C. The S-layer proteins of tannerella forsythia are secreted via a type IX secretion system that is decoupled from protein O-glycosylation. Mol Oral Microbiol 2014; 29:307-20; PMID:24943676; http://dx.doi.org/10.1111/omi.12062
  • Inagaki S, Onishi S, Kuramitsu HK, Sharma A. Porphyromonas gingivalis vesicles enhance attachment, and the leucine-rich repeat BspA protein is required for invasion of epithelial cells by tannerella forsythia. Infect Immun 2006; 74:5023-8; PMID:16926393; http://dx.doi.org/10.1128/IAI.00062-06
  • Larsbrink J, Rogers TE, Hemsworth GR, McKee LS, Tauzin AS, Spadiut O, Klinter S, Pudlo NA, Urs K, Koropatkin NM., et al. A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes. Nature 2014; 506:498-502; PMID:24463512; http://dx.doi.org/10.1038/nature12907
  • Martens EC, Koropatkin NM, Smith TJ, Gordon JI. Complex glycan catabolism by the human gut microbiota: the bacteroidetes sus-like paradigm. J Biol Chem 2009; 284:24673-7; PMID:19553672; http://dx.doi.org/10.1074/jbc.R109.022848
  • Thompson H, Homer KA, Rao S, Booth V, Hosie AH. An orthologue of bacteroides fragilis NanH is the principal sialidase in tannerella forsythia. J Bacteriol 2009; 191:3623-8; PMID:19304852; http://dx.doi.org/10.1128/JB.01618-08
  • Cheng HR, Jiang N. Extremely rapid extraction of DNA from bacteria and yeasts. Biotechnol Lett 2006; 28:55-9; PMID:16369876; http://dx.doi.org/10.1007/s10529-005-4688-z
  • Sambrook J, Fritsch EF, Maniatis T. Molecular cloning. New York, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 1989
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-5; PMID:5432063; http://dx.doi.org/10.1038/227680a0
  • Leonard R, Rendic D, Rabouille C, Wilson IB, Preat T, Altmann F. The drosophila fused lobes gene encodes an N-acetylglucosaminidase involved in N-glycan processing. J Biol Chem 2006; 281:4867-75; PMID:16339150; http://dx.doi.org/10.1074/jbc.M511023200
  • McIlvaine TA. A buffer solution for colorimetric comparison. J Biol Chem 1921; 49:183-6
  • Kurz S, Jin C, Hykollari A, Gregorich D, Giomarelli B, Vasta GR, Wilson IB, Paschinger K. Hemocytes and plasma of the eastern oyster (crassostrea virginica) display a diverse repertoire of sulfated and blood group A-modified N-glycans. J Biol Chem 2013; 288:24410-28; PMID:23824194; http://dx.doi.org/10.1074/jbc.M113.478933
  • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-54; PMID:942051; http://dx.doi.org/10.1016/0003-2697(76)90527-3
  • Honma K, Mishima E, Inagaki S, Sharma A. The OxyR homologue in tannerella forsythia regulates expression of oxidative stress responses and biofilm formation. Microbiol 2009; 155:1912-22; PMID:19389765; http://dx.doi.org/10.1099/mic.0.027920-0
  • Stafford P, Higham J, Pinnock A, Murdoch C, Douglas CW, Stafford GP, Lambert DW. Gingipain-dependent degradation of mammalian target of rapamycin pathway proteins by the periodontal pathogen porphyromonas gingivalis during invasion. Mol Oral Microbiol 2013; 28:366-78; PMID:23714361; http://dx.doi.org/10.1111/omi.12030

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