Characterization of hemin-binding of oral streptococci
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
Certain pathogenic bacteria obtain iron for growth through heme or heme compounds. Streptococci are gram-positive bacteria that reside in the mouth and require iron for growth. However, the iron accumulation mechanism in streptococci remains unknown. Therefore, this study investigated the hemin-binding properties of streptococci to confirm the potential of oral streptococci to obtain iron through heme compounds. The hemin-binding ability of streptococci was evaluated by incubation with hemin and subsequent measurement of the optical density of the supernatant to determine the amount of hemin bound by the bacteria using the hemin concentration standard curve. The hemin-binding of streptococci was proportional to the concentration of bacteria (Streptococcus gordonii) and hemin added. However, when a high hemin concentration of up to 60 μg/mL was added, the amount of hemin bound by S. gordonii remained almost unchanged. The incubation temperature had no significant effect on hemin-binding, but pretreatment with trypsin and protease decreased hemin-binding. Additionally, we experimentally confirmed that S. gordonii could use hemin for growth. This study demonstrated that streptococci possess hemin-binding sites and can acquire iron through hemin.
Abstract
Certain pathogenic bacteria obtain iron for growth through heme or heme compounds. Streptococci are gram-positive bacteria that reside in the mouth and require iron for growth. However, the iron accumulation mechanism in streptococci remains unknown. Therefore, this study investigated the hemin-binding properties of streptococci to confirm the potential of oral streptococci to obtain iron through heme compounds. The hemin-binding ability of streptococci was evaluated by incubation with hemin and subsequent measurement of the optical density of the supernatant to determine the amount of hemin bound by the bacteria using the hemin concentration standard curve. The hemin-binding of streptococci was proportional to the concentration of bacteria (Streptococcus gordonii) and hemin added. However, when a high hemin concentration of up to 60 μg/mL was added, the amount of hemin bound by S. gordonii remained almost unchanged. The incubation temperature had no significant effect on hemin-binding, but pretreatment with trypsin and protease decreased hemin-binding. Additionally, we experimentally confirmed that S. gordonii could use hemin for growth. This study demonstrated that streptococci possess hemin-binding sites and can acquire iron through hemin.
참고문헌 (32)
- Baddour LM, "Pathogenesis of experimental endocarditis", Rev Infect Dis, 11, pp.452~463 (1989)[DOI]
- Weinberg ED, "Iron and infection", Microbiol Rev, 42, pp.45~66 (1978)[DOI]
- Crichton RR, "Iron transport and storage", Eur J Biochem, 164, pp.485~506 (1987)[DOI]
- Bullen JJ, "Role of iron in bacterial infection", Curr Top Microbiol Immunol, 80, pp.1~35 (1978)[DOI]
- Moeck GS, "TonB-dependent iron acquisition : mechanisms of siderophore-mediated active transport", Mol Microbiol, 28, pp.675~681 (1998)[DOI]
- Snow GA, "Mycobactins : iron-chelating growth factors from mycobacteria", Bacteriol Rev, 34, pp.99~125 (1970)[DOI]
- Russell LM, "Initial characterization of the ferric iron transport system of Corynebacterium diphtheriae", J Bacteriol, 155, pp.1439~1442 (1983)[DOI]
- Adams TJ, "Iron acquisition systems of Listeria monocytogenes", Infect Immun, 58, pp.2715~2718 (1990)[DOI]
- Evans SL, "Ferrous iron transport in Streptococcus mutans", J Bacteriol, 168, pp.1096~1099 (1986)[DOI]
- Pettersson A, "Response of Neisseria meningitidis to iron limitation", Antonie Van Leeuwenhoek, 71, pp.129~136 (1997)[DOI]
- Schryvers AB, "Iron acquisition systems in the pathogenic Neisseria", Mol Microbiol, 32, pp.1117~1123 (1999)[DOI]
- Mickelsen PA, "Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds", Infect Immun, 33, pp.555~564 (1981)[DOI]
- Coulton JW, "Transport of hemin by Haemophilus influenzae type b", Curr Microbiol, 9, pp.93~97 (1983)[DOI]
- Bramanti TE, "Roles of porphyrins and host iron transport proteins in regulation of growth of Porphyromonas gingivalis W50", J Bacteriol, 173, pp.7330~7339 (1991)[DOI]
- Dashper SG, "Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis", J Bacteriol, 182, pp.6456~6462 (2000)[DOI]
- Xu X, "Cloning and expression of two novel hemin binding protein genes from Treponema denticola", Infect Immun, 69, pp.4465~4472 (2001)[DOI]
- Graber KR, "Expression of iron binding proteins and hemin binding activity in the dental pathogen Actinobacillus actinomycetemcomitans", FEMS Microbiol Lett, 163, pp.135~142 (1998)[DOI]
- Worst DJ, "Iron-repressible outer membrane proteins of Helicobacter pylori involved in heme uptake", Infect Immun, 63, pp.4161~4165 (1995)[DOI]
- Desai PJ, "Binding and accumulation of hemin in Neisseria gonorrhoeae", Infect Immun, 63, pp.4634~4641 (1995)[DOI]
- Stoebner JA, "Iron-regulated hemolysin production and utilization of heme and hemoglobin by Vibrio cholerae", Infect Immun, 56, pp.2891~2895 (1988)[DOI]
- Eichenbaum Z, "Acquisition of iron from host proteins by the group A streptococcus", Infect Immun, 64, pp.5428~5429 (1996)[DOI]
- Hamada S, "Biology, immunology, and cariogenicity of Streptococcus mutans", Microbiol Rev, 44, pp.331~384 (1980)[DOI]
- Deneer HG, "Effect of iron restriction on the outer membrane proteins of Actinobacillus(Haemophilus)pleuropneumoniae", Infect Immun, 57, pp.798~804 (1989)[DOI]
- Genco CA, "Binding and accumulation of hemin in Porphyromonas gingivalis are induced by hemin", Infect Immun, 62, pp.2885~2892 (1994)[DOI]
- Torres VJ, "Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization", J Bacteriol, 188, pp.8421~8429 (2006)[DOI]
- Eichenbaum Z, "Iron starvation causes release from the group A streptococcus of the ADPribosylating protein called plasmin receptor or surface glyceraldehyde-3-phosphate-dehydrogenase", Infect Immun, 64, pp.1956~1960 (1996)[DOI]
- Payne SM, "Iron and virulence in the family Enterobacteriaceae", Crit Rev Microbiol, 16, pp.81~111 (1988)[DOI]
- Tai SS, "Characterization of hemin binding activity of Streptococcus pneumoniae", Infect Immun, 65, pp.1083~1087 (1997)[DOI]
- Smalley JW, "Haemin binding as a factor in the virulence of Porphyromonas gingivalis", FEMS Microbiol Lett, 141, pp.65~70 (1996)[DOI]
- Grenoble DC, "The effect of pressure on the oxidation state of iron. 3. Hemin and hematin", Proc Natl Acad Sci U S A, 61, pp.1177~1182 (1968)[DOI]
- Morgan WT, "Porphyrin-binding proteins in serum", Ann N Y Acad Sci, 244, pp.624~650 (1975)[DOI]
- Bonkovsky HL, "Porphyrin and heme metabolism and the porphyrias", Compr Physiol, 3, pp.365~401 (2013)[DOI]