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Infection and Immunity, September 1998, p. 4511-4516, Vol. 66, No. 9
Department of Microbiology, University of
Texas Southwestern Medical Center, Dallas, Texas
75235-9048,1 and
Department of
Cellular Biochemistry, Institute of Haemotology and Blood
Transfusion, 128 20 Prague-2, Czech Republic2
Received 27 February 1998/Returned for modification 2 April
1998/Accepted 17 June 1998
Utilization of heme-hemopexin as a source of heme by
Haemophilus influenzae type b is dependent on
expression by this bacterium of the 100-kDa HxuA protein, which
is both present on the bacterial cell surface and released into the
culture supernatant (L. D. Cope, R. Yogev, U. Muller-Eberhard, and
E. J. Hansen, J. Bacteriol. 177:2644-2653, 1995).
Radioimmunoprecipitation analysis showed that the soluble HxuA
protein present in H. influenzae type b culture supernatant bound heme-hemopexin complexes in solution. An
isogenic H. influenzae type b
hxuA mutant was unable to utilize soluble heme-hemopexin
complexes for growth in vitro unless soluble HxuA protein was provided
exogenously. Soluble HxuA protein secreted by a nontypeable
H. influenzae strain also allowed growth of this H. influenzae type b hxuA mutant. These
results indicated that the heme present in heme-hemopexin
complexes is rendered accessible to H. influenzae when
these complexes are bound by the soluble HxuA protein.
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Binding of Heme-Hemopexin Complexes by Soluble HxuA Protein
Allows Utilization of This Complexed Heme by
Haemophilus influenzae
*
Corresponding author. Mailing address: Department
of Microbiology, University of Texas Southwestern Medical
Center, Hamon Biomedical Research Building, NA6.200A, 6000 Harry Hines
Blvd., Dallas, TX 75235-9048. Phone: (214) 648-5974. Fax: (214)
648-5905. E-mail: hansen01{at}utsw.swmed.edu.
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