Molecular cloning of haemoglobin-binding protein HgbA in the outer membrane of Actinobacillus pleuropneumoniae

Microbiology

Volumn 150, Issue 6, 2004, Pages 1723-1734

  Srikumar, Ramakrishnan ^a   Mikael, Leonie G ^b   Pawelek, Peter D ^a   Khamessan, Ali ^a   Gibbs, Bernard F ^c   Jacques, Mario ^b   Coulton, James W ^a  

^a MCGILL UNIVERSITY   (Canada)

^b UNIVERSITÉ DE MONTRÉAL   (Canada)

^c MDS Inc   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AGAROSE; AMINO ACID; HAPTOGLOBIN; HEMOGLOBIN A; OLIGONUCLEOTIDE; OUTER MEMBRANE PROTEIN; SIGNAL PEPTIDE;

ACTINOBACILLUS PLEUROPNEUMONIAE; AMPLICON; ANIMAL CELL; ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERIUM CULTURE; BINDING SITE; CONSENSUS SEQUENCE; CONTROLLED STUDY; CULTURE MEDIUM; DELETION MUTANT; ENZYME PURIFICATION; FLOW CYTOMETRY; GENE LIBRARY; GENETIC SCREENING; IRON DEFICIENCY; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PASTEURELLA MULTOCIDA; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ISOLATION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SEROTYPE; SWINE; UPREGULATION;

ACTINOBACILLUS; ACTINOBACILLUS PLEUROPNEUMONIAE; PASTEURELLA; PASTEURELLA MULTOCIDA; SUIDAE; SUS SCROFA;

EID: 3142694132     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.27046-0     Document Type: Article

References (40)

1. Archambault, M., Rioux, S. & Jacques, M. (1999). Evaluation of the hemoglobin-binding activity of Actinobacillus pleuropneumoniae using fluorescein-labeled pig hemoglobin and flow cytometry. FEMS Microbiol Lett 173, 17-25.
2. Archambault, M., Labrie, J., Rioux, C., Dumas, F., Thibault T., Elkins, C. & Jacques, M. (2003). Identification and preliminary characterization of a 75-kDa hemin- and hemoglobin-binding outer membrane protein of Actinobacillus pleuropneumoniae serotype 1. Can J Vet Res 67, 271-277.
3. Baltes, N., Tonpitak, W., Hennig-Pauka, I., Gruber, A. D. & Gerlach, G. F. (2003). Actinobacillus pleuropneumoniae serotype 7 siderophore receptor FhuA is not required for virulence. FEMS Microbiol Lett 220, 41-48.
4. Bélanger, M., Bégin, C. & Jacques, M. (1995). Lipopolysaccharides of Actinobacillus pleuropneumoniae bind pig hemoglobin. Infect Immun 63, 656-662.
5. Bosch, M., Garrido, M. E., Llagostera, M., de Rozas, M. P., Badiola, I. & Barbé, J. (2002). Characterization of the Pasteurella multocida hgbA gene encoding a hemoglobin-binding protein. Infect Immun 70, 5955-5964.
6. Bossé, J. T., Janson, H., Sheehan, B. J., Beddek, A. J., Rycroft, A. N., Kroll, S. & Langford, P. R. (2002). Actinobacillus pleuropneumoniae: pathobiology and pathogenesis of infection. Microbes Infect 4, 225-235.
7. Bracken, C. S., Baer, M. T., Abdur-Rashid, A., Helms, W. & Stojilikovic, I. (1999). Use of heme-protein complexes by the Yersinia enterocolitica HemR receptor: histidine residues are essential for receptor function. J Bacteriol 181, 6063-6072.
8. Buchanan, S. K., Smith, B. S., Venkatramani, L., Xia, D., Esser, L., Palnitkar, M., Chakraborty, R., van der Helm, D. & Deisenhofer, J. (1999). Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nat Struct Biol 6, 56-63.
9. Byers, B. R. & Arceneaux, J. E. L. (1998). Microbial iron transport: iron acquisition by pathogenic microorganisms. In Metal Ions in Biological Systems, Iron Transport and Storage in Microorganisms, Plants and Animals, vol. 35, pp. 37-66. Edited by A. Sigel & H. Sigel. New York: Marcel Dekker.
10. Dehio, C. & Meyer, M. (1997). Maintenance of broad-host-range incompatibility group P and Q plasmids and transposition of Tn5 in Bartonella henselae following conjugal transfer from Escherichia coli. J Bacteriol 179, 538-540.
11. Deneer, H. G. & Potter, A. A. (1989). Effect of iron restriction on the outer membrane proteins of Actinobacillus (Haemophilus) pleuropneumoniae. Infect Immun 57, 798-804.
12. Diarra, M. S., Dolence, J. A., Dolence, E. K., Darwish, I., Miller, M. J., Malouin, F. & Jacques, M. (1996). Growth of Actinobacillus pleuropneumoniae is promoted by exogenous hydroxamate and catecholate siderophores. Appl Environ Microbiol 62, 853-859.
13. D'Silva, C. G., Archibald, F. S. & Niven, D. F. (1995). Comparative study of iron acquisition by biotype 1 and biotype 2 strains of Actinobacillus pleuropneumoniae. Vet Microbiol 44, 11-23.
14. Eddy, S. R., Sonnhammer, E. L. L., Bateman, A., Birney, E., Durbin, R. & Howe, K. L. (2000). The Pfam protein families database. Nucleic Acids Res 28, 263-266.
15. Elkins, C., Chen, C. J. & Thomas, C. E. (1995). Characterization of hgbA locus encoding a hemoglobin receptor from H. ducreyi. Infect Immun 63, 2194-2220.
16. Fenwick, B. & Henry, S. (1994). Porcine pleuropneumonia. J Am Vet Med Assoc 204, 1334-1340.
17. Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K. & Welte, W. (1998). Siderophore-mediated iron transport: crystal structure of the FhuA with bound lipopolysaccharide. Science 282, 2215-2220.
18. Frey, J. (1992). Construction of a broad host range shuttle vector for gene cloning and expression in Actinobacillus pleuropneumoniae and other Pasteurellaceae. Res Microbiol 143, 263-269.
19. Genco, C. A. & Dixon, D. W. (2001). Emerging strategies in microbial haem capture. Mol Microbiol 39, 1-11.
20. Gerlach, G. F., Anderson, C., Potter, A. A., Klashinsky, S. & Willson, P. J. (1992). Cloning and expression of a transferrin-binding protein from Actinobacillus pleuropneumoniae. Infect Immun 60, 892-898.
21. Gonzalez, G. C., Yu, R.-Y., Rosteck, P. R. J. & Schryvers, A. B. (1995). Sequence, genetic analysis, and expression of Actinobacillus pleuropneumoniae transferrin receptor genes. Microbiology 141, 2405-2416.
22. Hanson, M. S. & Hansen, E. J. (1991). Molecular cloning of a haemin-binding lipoprotein from Haemophilus influenzae type b. Mol Microbiol 5, 267-278.
23. Lee, B. C. (1992). Isolation of an outer membrane haemin-binding protein of Haemophilus influenzae type b. Infect Immun 60, 810-816.
24. Lee, B. C. (1995). Quelling the red menace: haem capture by bacteria. Mol Microbiol 18, 383-390.
25. Litwin, C. M. & Calderwood, S. B. (1993). The role of iron in the regulation of virulence genes. Clin Microbiol Rev 6, 137-149.
26. Locher, K. P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J. P. & Moras, D. (1998). Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 95, 771-778.
27. Maciver, I., Latimer, J. L., Liem, H. H., Muller-Eberhard, U. Z., Hrkal, Z. & Hansen, E. J. (1996). Identification of an outer membrane protein involved in utilization of haemoglobin-haptoglobin complexes by nontypeable Haemophilus influenzae. Infect Immun 64, 3703-3712.
28. Mikael, L. G., Pawelek, P. D., Labrie, J., Sirois, M., Coulton, J. W. & Jacques, M. (2002). Molecular cloning and characterization of the ferric hydroxamate uptake (fhu) operon in Actinobacillus pleuropneumoniae. Microbiology 148, 2869-2882.
29. Mikael, L. G., Srikumar, R., Coulton, J. W. & Jacques, M. (2003). fhuA of Actinobacillus pleuropneumoniae encodes a ferrichrome receptor and is not regulated by iron. Infect Immun 71, 2911-2915.
30. Morton, D. J., Whitby, P. W., Jin, H., Ren, Z. & Stull, T. L. (1999). Effect of multiple mutations in hemoglobin- and hemoglobin-haptoglobin-binding proteins, HgpA, HgpB, and HgpC, of Haemophilus influenzae type b. Infect Immun 67, 2729-2739.
31. Niven, D. F., Donga, J. & Archibald, F. S. (1989). Responses of Haemophilus pleuropneumoniae to iron restriction; changes in the outer membrane protein profile and the removal of iron from porcine transferrin. Mol Microbiol 3, 1083-1089.
32. Oswald, W., Walaiporn, T., Ohrt, G. & Gerlach, G. F. (1999). A single-step transconjugation system for the introduction of unmarked deletions into Actinobacillus pleuropneumoniae serotype 7 using a sucrose sensitivity marker. FEMS Microbiol Lett 179, 153-160.
33. Otto, B. R., Verweij-Van Vught, A. M. J. J. & Maclaren, D. M. (1992). Transferrins and heme compounds as iron sources for pathogenic bacteria. Crit Rev Microbiol 18, 217-233.
34. Palmer, K. L., Grass, S. & Munson, R. S. (1994). Identification of a hemolyLic activity elaborated by Haemophilus ducreyi. Infect Immun 62, 3041-3043.
35. Simpson, W., Olczak, T. & Genco, C. A. (2000). Characterization and expression of HmuR, a TonB-dependent hemoglobin receptor of Porphyromonas gingivalis. J Bacteriol 182, 5737-5748.
36. Stojiljkovic, I., Larson, J., Hwa, V., Anic, S. & So, M. (1996). HmbR outer membrane receptors of pathogenic Neisseria spp. iron-regulated, hemoglobin -binding proteins with a high level of primary structure conservation. J Bacteriol 178, 4670-4678.
37. Vézina, G., Sirois, M., Clairoux, N. & Boissinot, M. (1997). Cloning and characterization of the groE locus from Actinobacillus pleuropneumoniae. FEMS Microbiol Lett 147, 11-16.
38. Wandersman, C. & Stojiljkovic, I. (2000). Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Curr Opin Microbiol 3, 215-220.
39. Williams, P. & Griffiths, E. (1992). Bacterial transferrin receptors: structure, function and contribution to virulence. Med Microbiol Immunol 181, 301-322.
40. Wilm, M., Shevchenko, A., Houthaeve, T., Brelt, S., Schwelgerer, L., Fotsis, T. & Mann, M. (1996). Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469.