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1 Department of Pediatrics, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA
2 Department of Microbiology/Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA
3 School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO 64110, USA
Correspondence
Terrence L. Stull
terrence-stull{at}ouhsc.edu
Haemophilus influenzae has an absolute growth requirement for a porphyrin source. This growth requirement can be satisfied in vitro by haem, haemoglobin or the haemoglobin–haptoglobin, haem–haemopexin and haem–albumin complexes. A family of proteins, termed the Hgp proteins, which are essential for utilization of the haemoglobin–haptoglobin complex, has previously been identified. A strain lacking the Hgp proteins also has a residual ability to utilize haemoglobin, indicating that additional moieties contribute to haemoglobin utilization. Using a haemoglobin affinity method an approximately 105 kDa protein was isolated. Mutation of the identified gene in an Hgp null background reduced the ability of the mutant strain to utilize haemoglobin in vitro. The mutation also resulted in a reduced ability to utilize haem, haem–haemopexin, haem–albumin and haemoglobin–haptoglobin, thus identifying a general haem-utilization protein (Hup) in Haemophilus influenzae.
The GenBank/EMBL/DDBJ accession numbers for the sequences reported in this paper are AY496274 for strain HI689 and AY525146 for strain E1a.
Present address: Amylin Pharmaceuticals, Inc., 9360 Towne Centre Drive, San Diego, CA 92121, USA.
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