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Infection and Immunity, October 2007, p. 4857-4866, Vol. 75, No. 10
0019-9567/07/$08.00+0     doi:10.1128/IAI.00407-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Passively Released Heme from Hemoglobin and Myoglobin Is a Potential Source of Nutrient Iron for Bordetella bronchiseptica{triangledown}

Jeffrey C. Mocny,1,2 John S. Olson,4 and Terry D. Connell1,2,3*

Department of Microbiology and Immunology,1 The Witebsky Center for Microbial Pathogenesis and Immunology,2 Department of Oral Biology, The University at Buffalo, Buffalo, New York,3 Department of Biochemistry & Cell Biology and The W. M. Keck Center for Computational Biology, Rice University, Houston, Texas4

Received 19 March 2007/ Returned for modification 31 May 2007/ Accepted 20 July 2007

Colonization by Bordetella bronchiseptica results in a variety of inflammatory respiratory infections, including canine kennel cough, porcine atrophic rhinitis, and a whooping cough-like disease in humans. For successful colonization, B. bronchiseptica must acquire iron (Fe) from the infected host. A vast amount of Fe within the host is sequestered within heme, a metalloporphyrin which is coordinately bound in hemoglobin and myoglobin. Utilization of hemoglobin and myoglobin as sources of nutrient Fe by B. bronchiseptica requires expression of BhuR, an outer membrane protein. We hypothesize that hemin is acquired by B. bronchiseptica in a BhuR-dependent manner after spontaneous loss of the metalloporphyrin from hemoglobin and/or myoglobin. Sequestration experiments demonstrated that direct contact with hemoglobin or myoglobin was not required to support growth of B. bronchiseptica in an Fe-limiting environment. Mutant myoglobins, each exhibiting a different affinity for heme, were employed to demonstrate that the rate of growth of B. bronchiseptica was directly correlated with the rate at which heme was lost from the hemoprotein. Finally, Escherichia coli cells expressing recombinant BhuR had the capacity to remove hemin from solution. Collectively, these experiments provided strong experimental support for the model that BhuR is a hemin receptor and B. bronchiseptica likely acquires heme during infection after passive loss of the metalloporphyrin from hemoglobin and/or myoglobin. These results also suggest that spontaneous hemin loss by hemoglobin and myoglobin may be a common mechanism by which many pathogenic bacteria acquire heme and heme-bound Fe.

* Corresponding author. Mailing address: 138 Farber Hall, Department of Microbiology and Immunology, The University at Buffalo, 3435 Main St., Buffalo, NY 14221. Phone: (716) 829-3364. Fax: (716) 829-2158. E-mail: connell{at}acsu.buffalo.edu

{triangledown} Published ahead of print on 30 July 2007.

Editor: V. J. DiRita

Infection and Immunity, October 2007, p. 4857-4866, Vol. 75, No. 10
0019-9567/07/$08.00+0     doi:10.1128/IAI.00407-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Allen, C. E., Schmitt, M. P. (2009). HtaA Is an Iron-Regulated Hemin Binding Protein Involved in the Utilization of Heme Iron in Corynebacterium diphtheriae. J. Bacteriol. 191: 2638-2648 [Abstract] [Full Text]  


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