Isolation and characterization of a hemin-binding cell envelope protein from Porphyromonas gingivalis

Microbial Pathogenesis

Volumn 21, Issue 1, 1996, Pages 65-70

  Kim, Sung Jo ^a   Chu, L ^a   Holt, S C ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

Hemin; Outer membranes; Porphyromonas gingivalis; TMBZ

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; CELL MEMBRANE PROTEIN; ENVELOPE PROTEIN; HEMIN; IRON;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; NONHUMAN; PORPHYROMONAS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ISOLATION;

BACTERIA (MICROORGANISMS); PORPHYROMONAS; PORPHYROMONAS GINGIVALIS;

EID: 0030200413     PISSN: 08824010     EISSN: None     Source Type: Journal    
DOI: 10.1006/mpat.1996.0043     Document Type: Article

References (20)

1. 1. Baura PK, Dyer DW, Neiders ME. Effect of iron limitation on Bacteroides gingivalis. Oral Microbiol Immunol 1990; 5: 263-8.
2. 2. Bramanti TE, Holt SC. Iron-regulated outer membrane proteins in the periodontopathic bacterium Bacteroides gingivalis. Biochem Biophys Res Commun 1990; 166: 1146-54.
3. 3. Chen CC, DeNardin A, Dyer DW, Neiders M. Human immunoglobulin G antibody response to iron-repressible and other membrane proteins of Porphyromonas (Bacteroides) gingivalis. Infect Immun 1991; 59: 2427-33.
4. 4. Papaioannou S, Marsh PD, Ivanyi L. The immunogenicity of outer membrane proteins of haemin-depleted Porphyromonas (Bacteroides) gingivalis W50 in periodontal disease. Oral Microbiol Immunol 1991; 6: 327-31.
5. 5. Smalley JW, Birss AJ, McKee AS, Marsh PD. Hemin-binding proteins of Porphyromonas gingivalis W50 grown in a chemostat under haemin-limitation. J Gen Microbiol 1993; 139: 2145-50.
6. 6. Grenier D. Hemin-binding property of Porphyromonas gingivalis outer membranes. FEMS Microbiol Lett 1991; 77: 45-50.
7. 7. Chu L, Song M, Holt SC. Effect of iron regulation on expression and hemin-binding function of outer sheath proteins from Treponema denticola. Microb Pathog 1994; 16: 321-35.
8. 8. Griffiths E, Stevenson P, Joyce P. Pathogenic Escherichia coli express new outer membrane proteins when growing in vivo. FEMS Microbiol Lett 1983; 16: 95-9.
9. 9. Maciver I, O'Reilly T, Brown MRW. Porphyrin ring source can alter the outer membrane protein of non-typeable Hemophilus influenzae. J Med Microbiol 1990; 31: 163-8.
10. 10. Otto BR, Sparrius M, Vermeij-van Vught AMJJ, MacLaren DM. Iron-regulated outer membrane protein of Bacteroides fragilis involved in heme uptake. Infect Immun 1990; 58: 3954-8.
11. 11. Williams P, Brown MRW. Influence of iron restriction on growth and the expression of outer membrane proteins by Hemophilus influenzae and H. parainfluenzae. FEMS Microbiol Lett 1985; 33: 153-7.
12. 12. Gibbons RJ, McDonald JB. Hemin and vitamin K compounds as required factors for the cultivation of certain strains of Bacteroides melaninogenicus. J Bacteriol 1960; 80: 164-70.
13. 13. Stugard CE, Daskaleros PA, Payne SM. A 101 kilodalton heme binding protein associated with Congo red binding and virulence of Shigella flexneri and enteroinvasive Escherichia coli strains. Infect Immun 1989; 57: 3534-9.
14. 14. Lee BC. Isolation of haemin-binding proteins of Neisseria gonorrhoeae. J Med Microbiol 1992; 36: 121-7.
15. 15. Hanson MS, Hansen EJ. Molecular cloning, partial purification, and characterization of a haemin-binding lipoprotein from Haemophilus influenzae type b. Mol Microbiol 1991; 5: 267-78.
16. 16. Hanson MS, Slaughter C, Hansen EJ. The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species. Infect Immun 1992; 60: 2257-66.
17. 17. Lee BC. Isolation of an outer membrane hemin-binding protein of Haemophilus influenzae type b. Infect Immun 1992; 60: 810-16.
18. 18. Bramanti TE, Holt SC. Hemin uptake in Porphyromonas gingivalis: Omp26 is a hemin-binding surface protein. J Bacteriol 1993; 175: 7413-20.
19. 19. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
20. 20. Hager DA, Burgess RR. Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with Sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topolsomerase, and other enzymes. Anal Biochem 1980; 109: 70-86.