| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, Alberta, Canada T2N 4N1
2Moredun Research Institute, International Research Centre, Pentlands Science Park, Bush Loan, Penicuik, Midlothian EH26 0PZ, UK
3Department of Microbiology3and First Department of Physiology
4, Kagawa Medical University, Kita-gun, Kagawa, 761–07, Japan
ABSTRACT
Summary: In a previous investigation, a 35 kDa iron-regulated protein was identified from total cellular proteins of Pasteurella haemolytica grown under iron-depleted conditions. This study reports identification of the gene (fbpA) encoding the 35 kDa protein based on complementation of an entA Escherichia coli strain transformed with a plasmid derived from a P. haemolytica lambda ZAP II library. Cross-reactivity was demonstrated between an anti-35 kDa mAb and a 35 kDa protein expressed in this strain. Furthermore, a translated ORF identified on the recombinant plasmid corresponded with the N-terminal amino acid sequence of the intact and a CNBr-cleaved fragment of the 35 kDa iron-regulated protein. Nucleotide sequence analysis of the gene encoding the 35 kDa protein demonstrated homology with the cluster 1 group of extracellular solute-binding proteins, especially to the iron-binding proteins of this family. Complete sequence analysis of the recombinant plasmid insert identified three other predominant ORFs, two of which appeared to be in an operonic organization with fbpA. These latter components (fbpB and fbpC) showed homology to the transmembrane and ATPase components of ATP-binding cassette (ABC)-type uptake systems, respectively. Based on amino acid/DNA sequencing, citrate competition assay of iron affinity and visible wavelength spectra, it was concluded that the P. haemolytica 35 kDa protein functions as an FbpA homologue (referred to as PFbpA) and that the gene encoding this protein is part of an operon comprising a member of the FbpABC family of iron uptake systems. Primary sequence analysis revealed rather surprisingly that PFbpA is more closely related to the intracellular Mn/Febinding protein IdiA found in cyanobacteria than to any of the homologous FbpA proteins currently known in commensal or pathogenic members of the Pasteurellaceae or Neisseriaceae.
Author for correspondence: S. D. Kirby. Tel: +1 403 2206047. Fax: +1 403 2702772. e-mail: sdkirby@acs.ucalgary.ca
This article has been cited by other articles:
|
|
 |
|
  E. E. Wyckoff, A. R. Mey, A. Leimbach, C. F. Fisher, and S. M. Payne Characterization of Ferric and Ferrous Iron Transport Systems in Vibrio cholerae. J. Bacteriol., September 1, 2006; 188(18): 6515 - 6523. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T.-C. Chao, J. Buhrmester, N. Hansmeier, A. Puhler, and S. Weidner Role of the Regulatory Gene rirA in the Transcriptional Response of Sinorhizobium meliloti to Iron Limitation Appl. Envir. Microbiol., October 1, 2005; 71(10): 5969 - 5982. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. R. Shouldice, D. E. McRee, D. R. Dougan, L. W. Tari, and A. B. Schryvers Novel Anion-independent Iron Coordination by Members of a Third Class of Bacterial Periplasmic Ferric Ion-binding Proteins J. Biol. Chem., February 18, 2005; 280(7): 5820 - 5827. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. K. Doyle, X. Zhang, V. L. Popov, and J. W. McBride An Immunoreactive 38-Kilodalton Protein of Ehrlichia canis Shares Structural Homology and Iron-Binding Capacity with the Ferric Ion-Binding Protein Family Infect. Immun., January 1, 2005; 73(1): 62 - 69. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. S. Anderson, P. Adhikari, A. J. Nowalk, C. Y. Chen, and T. A. Mietzner The hFbpABC Transporter from Haemophilus influenzae Functions as a Binding-Protein-Dependent ABC Transporter with High Specificity and Affinity for Ferric Iron J. Bacteriol., September 15, 2004; 186(18): 6220 - 6229. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. R. Shouldice, R. J. Skene, D. R. Dougan, G. Snell, D. E. McRee, A. B. Schryvers, and L. W. Tari Structural Basis for Iron Binding and Release by a Novel Class of Periplasmic Iron-Binding Proteins Found in Gram-Negative Pathogens J. Bacteriol., June 15, 2004; 186(12): 3903 - 3910. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. L. Lam, S. Kirby, and A. B. Schryvers Foreign signal peptides can constitute a barrier to functional expression of periplasmic proteins in Haemophilus influenzae Microbiology, November 1, 2003; 149(11): 3155 - 3164. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. R. Shouldice, D. R. Dougan, P. A. Williams, R. J. Skene, G. Snell, D. Scheibe, S. Kirby, D. J. Hosfield, D. E. McRee, A. B. Schryvers, et al. Crystal Structure of Pasteurella haemolytica Ferric Ion-binding Protein A Reveals a Novel Class of Bacterial Iron-binding Proteins J. Biol. Chem., October 17, 2003; 278(42): 41093 - 41098. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Tolle, K.-P. Michel, J. Kruip, U. Kahmann, A. Preisfeld, and E. K. Pistorius Localization and function of the IdiA homologue Slr1295 in the cyanobacterium Synechocystis sp. strain PCC 6803 Microbiology, October 1, 2002; 148(10): 3293 - 3305. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
