TY - JOUR
T1 - Binding of heme-hemopexin complexes by soluble HxuA protein allows utilization of this complexed heme by Haemophilus influenzae
AU - Cope, L. D.
AU - Thomas, S. E.
AU - Hrkal, Z.
AU - Hansen, E. J.
PY - 1998
Y1 - 1998
N2 - 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- Eherhard, 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.
AB - 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- Eherhard, 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.
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U2 - 10.1128/.66.9.4511-4516.1998
DO - 10.1128/.66.9.4511-4516.1998
M3 - Article
C2 - 9712810
AN - SCOPUS:0031662952
SN - 0019-9567
VL - 66
SP - 4511
EP - 4516
JO - Infection and immunity
JF - Infection and immunity
IS - 9
ER -