Molecular characterization of the structural gene for the lactoferrin receptor of the meningococcal strain H44/76

Microbial Pathogenesis

Volumn 17, Issue 6, 1994, Pages 395-408

  Pettersson, Annika ^a   Klarenbeek, Vincent ^a   Van Deurzen, Jolanda ^a   Poolman, Jan T ^b   Tommassen, Jan ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b NATIONAL INSTITUTE FOR PUBLIC HEALTH AND THE ENVIRONMENT   (Netherlands)

Author keywords

IbpA; IbpB; Iron regulation; Lactoferrin receptor; Meningococcus; Outer membrane protein; Topology

Indexed keywords

EID: 0028641362     PISSN: 08824010     EISSN: None     Source Type: Journal    
DOI: 10.1006/mpat.1994.1085     Document Type: Article

References (49)

1. Bullen JJ, Rogers HJ, Griffiths E. Bacterial iron metabolism in infection and immunity. In: Neilands JB, ed. Microbial iron metabolism: a comprehensive treatise. New York: Academic Press, Inc. 1974: 518-51.
2. Masson PL, Heremans JF, Dive CH. An iron-binding protein common to many external secretions. Clin Chim Acta 1966; 14: 735-9.
3. Weinberg ED. Iron and infection. Microbiol Rev 1978; 42: 45-66
4. Finkelstein RA, Sciortion CV, McIntosh MA. Role of iron in microbe-host interactions. Rev Infect Dis 1983; 5: S759-77.
5. Neilands JB. Microbial iron compounds. Annu Rev Biochem 1981; 50: 715-31.
6. Postle K. TonB and the gram-negative dilemma. Mol Microbiol 1990; 4: 2019-25.
7. West SEH, Sparling PF. Response of Neisseria gonorrhoeae to iron limitation: alterations in expression of membrane proteins without apparent siderophore production. Infect Immun 1985; 47: 388-94.
8. Mickelsen PA, Sparling PF. Ability of Neisseria gonorrhoeae. Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect Immun 1981; 33: 555-64.
9. Mickelsen PA, Blackman E, Sparling PF. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from lactoferrin. Infect Immun 1982; 35: 915-20.
10. Schryvers AB, Morris LJ. Identification and characterization of the transferrin receptor from Neisseria meningitidis. Mol Microbiol 1988; 2: 281-8.
11. Lee BC, Schryvers AB. Specificity of the lactoferrin and transferrin receptors in Neisseria gonorrhoeae. Mol Microbiol 1988; 2: 827-29.
12. Schryvers AB, Lee BC. Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae. Can J Microbiol 1989; 35: 409-15.
13. Cornelissen CN, Biswas GD, Tsai J, Paruchuri DK, Thompson SA, Sparling PF. Gonococcal transferrinbinding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors. J Bacteriol 1992; 174: 5788-97.
14. Legrain M, Mazarin V, Irwin SW et al. Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbpl and Tbp2. Gene 1993; 130: 73-80.
15. Irwin SW, Averil N, Cheng CY, Schryvers AB. Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis. Mol Microbiol 1993; 8: 1125-33.
16. Pettersson A, van der Ley P, Poolman JT, Tommassen J. Molecular characterization of the 98-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis. Infect Immun 1993; 61: 4724-33.
17. Pettersson A, Maas A, Tommassen J. Identification of the iroA gene product of Neisseria meningitidis as a lactoferrin receptor. J Bacteriol 1994; 176: 1764-66.
18. Simonson C, Brener D, DeVoe IW. Expression of a high-affinity mechanism for acquisition of transferin iron by Neisseria meningitidis, infect Immun 1982; 36: 107-13.
19. Chen C-Y, Berish SA, Morse SA, Mietzner TA. The ferric iron-binding protein of Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin. Mol Microbiol 1993; 10: 311-18.
20. Ames GFL. Bacterial periplasmic transport systems: structure, mechanism and evolution. Annu Rev Biochem 1986; 55: 397-425.
21. Black JR, Dyer DW, Thompson MK, Sparling PF. Human immune response to iron-repressible outer membrane proteins of Neisseria meningitidis. Infect Immun 1986; 54: 710-13.
22. Struyve M, Moons M, Tommassen J. Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol 1991; 218:141-8.
23. Cowan SW, Schirmer T, Rummel G et al. Crystal structures explain functional properties of two E. coli porins. Nature 1992; 358: 727-33.
24. Weiss MS, Kreusch A, Schilz E et al. The structure of porin from Rhodobacter capsulatus at 1.8 fi resolution. FEBS Letters 1991; 280: 379-82.
25. Tommassen J. Biogenesis and membrane topology of outer membrane proteins in Escherichia coli. In: Op den Kamp JAF, ed. Membrane biogenesis. NATO ASI Series, Vol H16. Berlin: Springer-Verlag KG. 1988:351-73.
26. van der Ley P, Struyve M, Tommassen J. Topology of outer membrane pore protein PhoE of Escherichia coli. Identification of cell surface-exposed amino acids with the aid of monoclonal antibodies. J Biol Chem 1986; 261: 12222-5.
27. Murphy CK, Kalve VI, Klebba PE. Surface topology of the Escherichia coii K-12 ferric enterobactin receptor. J Bacteriol 1990; 172: 2736-46.
28. Koebnik R, Braun V. Insertion derivatives containing segments of up to 16 amino acids identify surface- and periplasm-exposed regions of the FhuA outer membrane receptor of Escherichia coli K-12. J Bacteriol 1993; 175: 826-39.
29. Brok RGPM, Brinkman E, van Boxtel R, Bekkers ACAPA, Verheij HM, Tommassen J. Molecular characterization of enterobacterial pldA genes encoding outer membrane phospholipase A. J Bacteriol 1994; 176: 861-70.
30. Paul C, Rosenbusch JP. Folding patterns of porin and bacteriorhodopsin. EMBO J, 1985; 4: 1593-7.
31. Bagg A, Neilands JB. Ferric uptake regulation protein acts as a repressor, employing iron(ll) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 1987: 5471-7.
32. Berish SA, Subbarao S, Chen C-Y, Trees DL, Morse SA. Identification and cloning of a fur homolog from Neisseria gonorrhoeae. Infect Immun 1993; 61: 4599-4606.
33. Thomas CE, Sparling PF. Identification and cloning of a fur homologue from Neisseria meningitidis. Mol Microbiol 1994; 11: 725-37.
34. Heller K, Kadner RJ, Günter K. Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB- dependent receptor protein in the outer membraner of Escherichia coli. Gene 1988; 64: 147-53.
35. Bitter W, Tommassen J, Weisbeek P. Identification and characterization of the exbB, exbD and tonB genes of Pseudomonas putida WC358: their involvement in ferric-pseudobactin transport. Mol Microbiol 1993; 7: 117-30.
36. Koster M, van de Vossenberg J, Leong J, Weisbeek PJ. Identification and characterization of the pupB gene encoding an inducible ferric-pseudobactin receptor of Pseudomonas putida. Mol Microbiol 1993; 8: 591-601.
37. Rutz JM, Liu J, Lyons JA, et al. Formation of a gated channel by a ligand-specific transport protein in the bacterial outer membrane. Science 1992; 258: 471-5.
38. Young RA, Davis RW. Yeast RNA polymerase II genes: isolation with antibody probes. Science 1983; 222:778-82.
39. Bitter W, de Boer J, Zomer HWM, Koster MC, Weisbeek PJ, Tommassen J. Localisation of functional domains in the Escherichia coli coprogen receptor FhuEandthe Pseudomonas putida ferric-pseudobactin 358 receptor PupA. Mol Gen Genet, in press.
40. Yanisch-Perron C, Vieira J, Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUCl9 vectors. Gene 1985; 33: 103-19.
41. Sambrook J, Fritsch EF, Maniatis T. Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1989.
42. Gutierrez C, Devedjian JC. A plasmid facilitating in vitro construction of phoA gene fusions in Escherichia coli. Nucl Acids Res 1989; 17: 3999.
43. Hantke K. Cloning the repressor gene of iron-regulated systems in Escherichia coli K 12. Mol Gen Genet 1984: 197: 337-41.
44. Ausubel FM, Brent R, Kingston RE, et al. Current protocols in molecular biology. Brooklyn, NY: Greene Publishing Associates, 1989.
45. Snyder M, Elledge SE, Sweetser D, Young RA, Davis RW. xgtll: gene isolation with antibody probes and other applications. Methods Enzymol 1987; 154: 107-28.
46. Wiertz EJHJ, vangaans-vanden Brink JAM, Gausepohl H, Prochinka-Chalufour A, Hoogerhout P, Poolman JT. Identification of T cell epitopes occurring in a meningococcal Class 1 outer membrane protein using overlapping peptides assembled with simultaneous multiple peptide synthesis. J Exp Med 1992;176:79-88.
47. Abdillahi H, Poolman JT. Whole-cell ELISA fortyping Neisseria meningitidis with monoclonal antibodies. FEMS Microbiol Lett 1987; 48: 367-71.
48. Tommassen J, Lugtenberg B. Outer membrane protein e of Escherichia coli K-12 is co-regulated with alkaline phosphatase. J Bacteriol 1980; 143: 151-7.
49. Miller JH. Experiments in molecular genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1972