This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Lee, B C Search for Related Content PubMed PubMed Citation Articles by Lee, B C

 Previous Article  |  Next Article 

Infect Immun. 1992 March; 60(3): 810-816

Isolation of an outer membrane hemin-binding protein of Haemophilus influenzae type b.

Department of Microbiology and Infectious Diseases, University of Calgary, Alberta, Canada.

ABSTRACT

Haemophilus influenzae is a heme-dependent bacterium. However, little is known of the heme-iron uptake mechanism in this organism. By using a batch ligand affinity chromatography method, a hemin-binding protein of 39,500 molecular weight was isolated from total membranes derived from H. influenzae type b grown under iron-depleted but not under iron-sufficient conditions. Detection of the hemin-binding protein in a whole-cell binding assay demonstrated a surface-exposed location. Competition binding experiments indicated that this hemin-protein interaction was specific, since only hemin or heme-containing proteins, such as human hemoglobin and bovine catalase, but not protoporphyrin IX, iron-loaded human lactoferrin, or transferrin, could abrogate binding. In a limited survey of other H. influenzae strains, an identical hemin-binding protein was isolated, implying that this polypeptide may be structurally and functionally conserved among strains.

This article has been cited by other articles:

• Asuthkar, S., Velineni, S., Stadlmann, J., Altmann, F., Sritharan, M. (2007). Expression and Characterization of an Iron-Regulated Hemin-Binding Protein, HbpA, from Leptospira interrogans Serovar Lai. Infect. Immun. 75: 4582-4591 [Abstract] [Full Text]  
• Ahn, S.-H., Han, J.-H., Lee, J.-H., Park, K.-J., Kong, I.-S. (2005). Identification of an Iron-Regulated Hemin-Binding Outer Membrane Protein, HupO, in Vibrio fluvialis: Effects on Hemolytic Activity and the Oxidative Stress Response. Infect. Immun. 73: 722-729 [Abstract] [Full Text]  
• Srikumar, R., Mikael, L. G., Pawelek, P. D., Khamessan, A., Gibbs, B. F., Jacques, M., Coulton, J. W. (2004). Molecular cloning of haemoglobin-binding protein HgbA in the outer membrane of Actinobacillus pleuropneumoniae. Microbiology 150: 1723-1734 [Abstract] [Full Text]  
• Hirayama, M., Kobiyama, A., Kinoshita, S., Watabe, S. (2004). The occurrence of two types of hemopexin-like protein in medaka and differences in their affinity to heme. J. Exp. Biol. 207: 1387-1398 [Abstract] [Full Text]  
• Zimmermann, R., Kempf, V. A. J., Schiltz, E., Oberle, K., Sander, A. (2003). Hemin Binding, Functional Expression, and Complementation Analysis of Pap 31 from Bartonella henselae. J. Bacteriol. 185: 1739-1744 [Abstract] [Full Text]  
• Xu, X., Holt, S. C., Kolodrubetz, D. (2001). Cloning and Expression of Two Novel Hemin Binding Protein Genes from Treponema denticola. Infect. Immun. 69: 4465-4472 [Abstract] [Full Text]  
• Dashper, S. G., Hendtlass, A., Slakeski, N., Jackson, C., Cross, K. J., Brownfield, L., Hamilton, R., Barr, I., Reynolds, E. C. (2000). Characterization of a Novel Outer Membrane Hemin-Binding Protein of Porphyromonas gingivalis. J. Bacteriol. 182: 6456-6462 [Abstract] [Full Text]  
• Ren, Z., Jin, H., Morton, D. J., Stull, T. L. (1998). hgpB, a Gene Encoding a Second Haemophilus influenzae Hemoglobin- and Hemoglobin-Haptoglobin-Binding Protein. Infect. Immun. 66: 4733-4741 [Abstract] [Full Text]  
• Thomas, C. E., Olsen, B., Elkins, C. (1998). Cloning and Characterization of tdhA, a Locus Encoding a TonB-Dependent Heme Receptor from Haemophilus ducreyi. Infect. Immun. 66: 4254-4262 [Abstract] [Full Text]  
• Cope, L. D., Thomas, S. E., Hrkal, Z., Hansen, E. J. (1998). Binding of Heme-Hemopexin Complexes by Soluble HxuA Protein Allows Utilization of This Complexed Heme by Haemophilus influenzae. Infect. Immun. 66: 4511-4516 [Abstract] [Full Text]