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J Oral Microbiol
v.3; 2011
PMC3087192
J Oral Microbiol. 2011; 3: 10.3402/jom.v3i0.5660.
Published online 2011 Jan 12. doi: 10.3402/jom.v3i0.5660
Groupe de Recherche en Écologie Buccale, Faculté de Médecine Dentaire, Université Laval, Québec, Canada
* Daniel Grenier , Groupe de Recherche en Écologie Buccale, Faculté de médecine dentaire, Université Laval, 2420 de la Terrasse, Quebec City, Québec G1V 0A6, Canada. Tel: +1 418 656 7341. Fax: +1 418 656 2861. Email: ac.lavalu.berg@reinerG.leinaD
Received 2010 Sep 22; Revised 2010 Dec 7; Accepted 2010 Dec 8.
Copyright © 2011 Daniel Grenier and Shin-ichi Tanabe
This is an Open Access article distributed under the terms of the Creative Commons Attribution-Noncommercial 3.0 Unported License, permitting all non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
This article has been cited by other articles in PMC.
Keywords: Periodontitis, Campylobacter rectus, transferrin, iron
a
Mean±standard deviation of triplicate assays.
1. Dewhirst FE, Chen T, Izard J, Paster BJ, Tanner AC, Yu WH, et al. The human oral microbiome. J Bacteriol. 2010; 192 :5002–17. [ PMC free article ] [ PubMed ] [ Google Scholar ]
2. Nishihara T, Koseki T. Microbial etiology of periodontitis. Periodontol 2000. 2004; 36 :14–26. [ PubMed ] [ Google Scholar ]
3. Macuch PJ, Tanner ACR.
Campylobacter rectus in health, gingivitis, and periodontitis. J Dent Res. 2000; 79 :785–92. [ PubMed ] [ Google Scholar ]
4. Suda R, Kobayashi M, Namba R, Iwamaru M, Hayashi Y, Lai CH, et al. Possible periodontal pathogens associated with clinical symptoms of periodontal disease in Japanese high school students. J Periodontol. 2004; 75 :1084–9. [ PubMed ] [ Google Scholar ]
5. Siqueira JF, Rocas IN.
Campylobacter gracilis and Campylobacter rectus in primary endodontic infections. Int Endod J. 2003; 36 :174–80. [ PubMed ] [ Google Scholar ]
6. Arce RM, Diaz PI, Barros SP, Galloway P, Bobetsis Y, Threadgill D, et al. Characterization of the invasive and inflammatory traits of oral Campylobacter rectus in a murine model of fetoplacental growth restriction and in trophoblast cultures. J Reprod Immunol. 2009; 84 :145–53. [ PMC free article ] [ PubMed ] [ Google Scholar ]
7. Williams P, Griffiths E. Bacterial transferrin receptors – structure, function and contribution to virulence. Med Microbiol Immunol. 1992; 181 :301–22. [ PubMed ] [ Google Scholar ]
8. Wooldridge KG, Williams PH. Iron uptake mechanisms of pathogenic bacteria. FEMS Microbiol Rev. 1993; 12 :325–48. [ PubMed ] [ Google Scholar ]
9. Curtis MA, Sterne JAC, Price SJ, Griffiths GS, Coulthurst SK, Wilton JMA, et al. The protein composition of gingival crevicular fluid sampled from male adolescents with no destructive periodontitis: baseline data of a longitudinal study. J Periodontal Res. 1990; 25 :6–16. [ PubMed ] [ Google Scholar ]
10. Goulet V, Britigan B, Nakayama K, Grenier D. Cleavage of human transferrin by Porphyromonas gingivalis gingipains promotes growth and formation of hydroxyl radicals. Infect Immun. 2004; 72 :4351–6. [ PMC free article ] [ PubMed ] [ Google Scholar ]
11. Duchesne P, Grenier D, Mayrand D. Binding and utilization of human transferrin by Prevotella nigrescens
. Infect Immun. 1999; 67 :576–80. [ PMC free article ] [ PubMed ] [ Google Scholar ]
12. Brochu V, Grenier D, Nakayama K, Mayrand D. Acquisition of iron from human transferrin by Porphyromonas gingivalis : a role for Arg- and Lys-gingipain activities. Oral Microbiol Immunol. 2001; 16 :79–87. [ PubMed ] [ Google Scholar ]
13. Makey DG, Seal US. The detection of four molecular forms of human transferrin during the iron binding process. Biochim Biophys Acta. 1976; 453 :250–6. [ PubMed ] [ Google Scholar ]
14. Pintor M, Ferreiros CM, Criado MT. Characterization of the transferrin-iron uptake system in Neisseria meningitidis
. FEMS Microbiol Lett. 1993; 112 :159–65. [ PubMed ] [ Google Scholar ]
15. Simonson C, Brener D, DeVoe IW. Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis
. Infect Immun. 1982; 36 :107–13. [ PMC free article ] [ PubMed ] [ Google Scholar ]
16. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193 :265–75. [ PubMed ] [ Google Scholar ]
17. Morrissey JA, Williams PH, Cashmore AM.
Candida albicans has a cell-associated ferric-reductase activity which is regulated in response to levels of iron and copper. Microbiology. 1996; 142 :485–92. [ PubMed ] [ Google Scholar ]
18. Grenier D, Goulet V, Mayrand D. The capacity of Porphyromonas gingivalis to multiply under iron-limiting conditions correlates with its pathogenicity in an animal model. J Dent Res. 2001; 80 :1678–82. [ PubMed ] [ Google Scholar ]
19. Rhodes ER, Menke S, Shoemaker C, Tomaras AP, McGillivary G, Actis LA. Iron acquisition in the dental pathogen Actinobacillus actinomycetemcomitans : what does it use as a source and how it get this essential metal? Biometals. 2007; 20 :365–77. [ PubMed ] [ Google Scholar ]
20. Xu X, Kolodrubetz D. Construction and analysis of hemin binding protein mutants in the oral pathogen Treponema denticola
. Res Microbiol. 2002; 153 :569–77. [ PubMed ] [ Google Scholar ]
21. Schenkein HA, Genco RJ. Gingival fluid and serum in periodontal diseases. J Periodontol. 1977; 48 :772–7. [ PubMed ] [ Google Scholar ]
22. Crossley RA, Gaskin DJH, Holmes K, Mulholland F, Wells JM, Kelly DJ, et al. Riboflavin biosynthesis is associated with assimilatory ferric reduction and iron acquisition by Campylobacter jejuni
. Appl Environ Microbiol. 2007; 73 :7819–25. [ PMC free article ] [ PubMed ] [ Google Scholar ]
23. Knight SAB, Vilaire G, Lesuisse E, Dancis A. Iron acquisition from transferrin by Candida albicans depends on the reductive pathway. Infect Immun. 2005; 73 :5482–92. [ PMC free article ] [ PubMed ] [ Google Scholar ]
24. Timmerman MM, Woods JP. Potential role of extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum
. Infect Immun. 2001; 69 :7671–8. [ PMC free article ] [ PubMed ] [ Google Scholar ]
Articles from Journal of Oral Microbiology are provided here courtesy of Taylor & Francis
1. Dewhirst FE, Chen T, Izard J, Paster BJ, Tanner AC, Yu WH, et al. The human oral microbiome. J Bacteriol. 2010; 192 :5002–17. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
2. Nishihara T, Koseki T. Microbial etiology of periodontitis. Periodontol 2000. 2004; 36 :14–26. [ PubMed ] [ Google Scholar ] [ Ref list ]
3. Macuch PJ, Tanner ACR.
Campylobacter rectus in health, gingivitis, and periodontitis. J Dent Res. 2000; 79 :785–92. [ PubMed ] [ Google Scholar ] [ Ref list ]
4. Suda R, Kobayashi M, Namba R, Iwamaru M, Hayashi Y, Lai CH, et al. Possible periodontal pathogens associated with clinical symptoms of periodontal disease in Japanese high school students. J Periodontol. 2004; 75 :1084–9. [ PubMed ] [ Google Scholar ] [ Ref list ]
5. Siqueira JF, Rocas IN.
Campylobacter gracilis and Campylobacter rectus in primary endodontic infections. Int Endod J. 2003; 36 :174–80. [ PubMed ] [ Google Scholar ] [ Ref list ]
6. Arce RM, Diaz PI, Barros SP, Galloway P, Bobetsis Y, Threadgill D, et al. Characterization of the invasive and inflammatory traits of oral Campylobacter rectus in a murine model of fetoplacental growth restriction and in trophoblast cultures. J Reprod Immunol. 2009; 84 :145–53. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
7. Williams P, Griffiths E. Bacterial transferrin receptors – structure, function and contribution to virulence. Med Microbiol Immunol. 1992; 181 :301–22. [ PubMed ] [ Google Scholar ] [ Ref list ]
8. Wooldridge KG, Williams PH. Iron uptake mechanisms of pathogenic bacteria. FEMS Microbiol Rev. 1993; 12 :325–48. [ PubMed ] [ Google Scholar ] [ Ref list ]
9. Curtis MA, Sterne JAC, Price SJ, Griffiths GS, Coulthurst SK, Wilton JMA, et al. The protein composition of gingival crevicular fluid sampled from male adolescents with no destructive periodontitis: baseline data of a longitudinal study. J Periodontal Res. 1990; 25 :6–16. [ PubMed ] [ Google Scholar ] [ Ref list ]
10. Goulet V, Britigan B, Nakayama K, Grenier D. Cleavage of human transferrin by Porphyromonas gingivalis gingipains promotes growth and formation of hydroxyl radicals. Infect Immun. 2004; 72 :4351–6. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
12. Brochu V, Grenier D, Nakayama K, Mayrand D. Acquisition of iron from human transferrin by Porphyromonas gingivalis : a role for Arg- and Lys-gingipain activities. Oral Microbiol Immunol. 2001; 16 :79–87. [ PubMed ] [ Google Scholar ] [ Ref list ]
11. Duchesne P, Grenier D, Mayrand D. Binding and utilization of human transferrin by Prevotella nigrescens
. Infect Immun. 1999; 67 :576–80. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
13. Makey DG, Seal US. The detection of four molecular forms of human transferrin during the iron binding process. Biochim Biophys Acta. 1976; 453 :250–6. [ PubMed ] [ Google Scholar ] [ Ref list ]
14. Pintor M, Ferreiros CM, Criado MT. Characterization of the transferrin-iron uptake system in Neisseria meningitidis
. FEMS Microbiol Lett. 1993; 112 :159–65. [ PubMed ] [ Google Scholar ] [ Ref list ]
15. Simonson C, Brener D, DeVoe IW. Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis
. Infect Immun. 1982; 36 :107–13. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
16. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193 :265–75. [ PubMed ] [ Google Scholar ] [ Ref list ]
17. Morrissey JA, Williams PH, Cashmore AM.
Candida albicans has a cell-associated ferric-reductase activity which is regulated in response to levels of iron and copper. Microbiology. 1996; 142 :485–92. [ PubMed ] [ Google Scholar ] [ Ref list ]
18. Grenier D, Goulet V, Mayrand D. The capacity of Porphyromonas gingivalis to multiply under iron-limiting conditions correlates with its pathogenicity in an animal model. J Dent Res. 2001; 80 :1678–82. [ PubMed ] [ Google Scholar ] [ Ref list ]
20. Xu X, Kolodrubetz D. Construction and analysis of hemin binding protein mutants in the oral pathogen Treponema denticola
. Res Microbiol. 2002; 153 :569–77. [ PubMed ] [ Google Scholar ] [ Ref list ]
21. Schenkein HA, Genco RJ. Gingival fluid and serum in periodontal diseases. J Periodontol. 1977; 48 :772–7. [ PubMed ] [ Google Scholar ] [ Ref list ]
22. Crossley RA, Gaskin DJH, Holmes K, Mulholland F, Wells JM, Kelly DJ, et al. Riboflavin biosynthesis is associated with assimilatory ferric reduction and iron acquisition by Campylobacter jejuni
. Appl Environ Microbiol. 2007; 73 :7819–25. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
23. Knight SAB, Vilaire G, Lesuisse E, Dancis A. Iron acquisition from transferrin by Candida albicans depends on the reductive pathway. Infect Immun. 2005; 73 :5482–92. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
24. Timmerman MM, Woods JP. Potential role of extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum
. Infect Immun. 2001; 69 :7671–8. [ PMC free article ] [ PubMed ] [ Google Scholar ] [ Ref list ]
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Campylobacter rectus is considered as one of the bacterial species of etiological importance in periodontitis. Iron-containing proteins such as transferrin are found in periodontal sites and may serve as a source of iron for periodontopathogens. The aim of this study was to investigate the capacity of C. rectus to assimilate transferrin-bound iron to support its growth.
Growth studies were performed in broth media pretreated with an iron-chelating resin and supplemented with various iron sources. The uptake of iron by C. rectus was monitored using 55 Fe-transferrin. Transferrin-binding activity was assessed using a microplate assay while the degradation of transferrin and iron removal was evaluated by polyacrylamide gel electrophoresis. A colorimetric assay was used to determine ferric reductase activity.
Holotransferrin (iron-saturated form) but not apotransferrin (iron-free form) was found to support growth of C. rectus in an iron-restricted culture medium. Incubation of holotransferrin with cells of C. rectus resulted in removal of iron from the protein. A time dependent intracellular uptake of iron by C. rectus cells from 55 Fe-transferrin was demonstrated. This uptake was significantly increased when bacteria were grown under an iron-limiting condition. Cells of C. rectus did not show transferrin-binding activity or proteolytic activity toward transferrin. However, a surface-associated ferric reductase activity was demonstrated.
To survive and multiply in periodontal sites, periodontopathogens must possess efficient iron-scavenging mechanisms. In this study, we showed the capacity of C. rectus to assimilate iron from transferrin to support its growth. The uptake of iron appears to be dependent on a ferric reductive pathway.
Periodontitis, a destructive chronic inflammatory disease, results from a polymicrobial infection and is characterized by the destruction of tooth-supporting tissues including the alveolar bone. Although more than 700 bacterial species are found in the oral cavity ( 1 ), a group of about 10 bacterial species has been strongly associated with periodontitis ( 2 ). There is now a consensus that Campylobacter rectus is a member of this group ( 3 ). Indeed, the proportions and levels of C. rectus are higher in periodontitis sites compared with healthy sites ( 3 , 4 ). This Gram-negative anaerobic bacterium is also frequently recovered from root canal infections ( 5 ). Very recently, Arce et al. ( 6 ) demonstrated that C. rectus has the ability to translocate in vivo from a distant site of infection to the placenta suggesting that it may be an important contributor to adverse pregnancy outcomes associated with periodontal disease.
Iron is a constituent of important metabolic enzymes and is essential for the growth of almost all microorganisms. Consequently, a critical virulence determinant of microorganisms is their ability to obtain iron from their hosts. Although there is an abundance of iron in the extracellular tissue fluids of human, the amount of free ionic iron (10 –18 M) is far too low to support growth of most bacteria ( 7 , 8 ). Transferrin is a serum glycoprotein possessing two iron-binding sites and is important in vivo for rendering iron unavailable to bacteria ( 7 ). Transferrin as well as other iron-containing proteins, including hemoglobin and lactoferrin, are known constituents of gingival crevicular fluid ( 9 ). In addition, Goulet et al. ( 10 ) reported that gingival crevicular fluid samples obtained from periodontitis patients show the presence of both transferrin and transferrin fragments, which amounts are correlated with the severity of the disease. Therefore, in the course of periodontitis, transferrin may represent an important source of iron for periodontopathogens.
Different mechanisms by which periodontopathogens can acquire iron from human transferrin to support their growth have been previously described ( 10 – 12 ). Prevotella nigrescens and Prevotella intermedia possess cell surface receptors with the capacity to bind transferrin ( 11 ). Porphyromonas gingivalis produces arginine-x-specific and lysine-x-specific gingipains that mediate a proteolytic cleavage of transferrin resulting in disruption of the iron-binding sites with the subsequent release and uptake of free iron ( 10 , 12 ). The aim of this study was to investigate the capacity of C. rectus to assimilate transferrin-bound iron to support its growth.
C. rectus ATCC 33238 was routinely grown in mycoplasma broth base (BBL Microbiology Systems, Cockeysville, MD), which was supplemented with 0.2% glucose, 0.2% sodium formate, and 0.2% sodium fumarate (MBB-GFF). Growth studies were performed using the above medium treated with the chelating resin (3 g/100 ml) Chelex 100 (Bio-Rad Laboratories, Mississauga, Ontario) for 2 h at room temperature with constant agitation. This iron-restricted medium was supplemented with either ferrous sulfate, human apotransferrin (iron-free form), or human holotransferrin (iron-saturated form), all at 20 µM and obtained from Sigma-Aldrich Canada (Oakville, Ontario, Canada). Cultures were incubated at 37°C in an anaerobic chamber (N 2 :H 2 :CO 2 /80:10:10). Bacterial growth was evaluated after 48 h of incubation by measuring the optical density at 660 nm (OD 660 ).
Equal volumes of holotransferrin (0.5 mg/ml) and C. rectus cells (OD 660 =0.5), treated or not at 60°C for 30 min, were incubated at room temperature for 2 h. Removal of iron from human holotransferrin was determined by urea/borate/EDTA-polyacrylamide gel electrophoresis (PAGE) analysis and Coomassie Blue staining ( 13 ). This electrophoretic procedure allows the differentiation of transferrin in the apo- (iron-free) and holo- (iron-saturated) forms.
The 55 Fe-transferrin was prepared based on the protocols of Pintor et al. ( 14 ) and Simonson et al. ( 15 ) using human apotransferrin and [ 55 Fe]FeCl 3 (NEN Life Science Products Inc., Boston, MA). Apotransferrin at 1 mg/ml was m
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Belle jeune se filme en train de se masturber
Elle aime passer de bite en bite