Abstract

Doc number: 166

Abstract

Background: Haemophilus influenzae requires a porphyrin source for aerobic growth and possesses multiple mechanisms to obtain this essential nutrient. This porphyrin requirement may be satisfied by either heme alone, or protoporphyrin IX in the presence of an iron source. One protein involved in heme acquisition by H. influenzae is the periplasmic heme binding protein HbpA. HbpA exhibits significant homology to the dipeptide and heme binding protein DppA of Escherichia coli . DppA is a component of the DppABCDF peptide-heme permease of E. coli . H. influenzae homologs of dppBCDF are located in the genome at a point distant from hbpA . The object of this study was to investigate the potential role of the H. influenzae dppBCDF locus in heme utilization.

Findings: An insertional mutation in dppC was constructed and the impact of the mutation on the utilization of both free heme and various proteinaceous heme sources as well as utilization of protoporphyrin IX was determined in growth curve studies. The dppC insertion mutant strain was significantly impacted in utilization of all tested heme sources and protoporphyin IX. Complementation of the dppC mutation with an intact dppCBDF gene cluster in trans corrected the growth defects seen in the dppC mutant strain.

Conclusion: The dppCBDF gene cluster constitutes part of the periplasmic heme-acquisition systems of H. influenzae .

Details

Title
The dppBCDF gene cluster of Haemophilus influenzae : Role in heme utilization
Author
Morton, Daniel J; Seale, Thomas W; VanWagoner, Timothy M; Whitby, Paul W; Stull, Terrence L
Pages
166
Publication year
2009
Publication date
2009
Publisher
BioMed Central
e-ISSN
17560500
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
1455079878
Copyright
© 2009 Morton et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.