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Characterization of a ferric‐binding protein mutant in Haemophilus influenzae
Author(s) -
Kirby Shane D.,
GrayOwen Scott D.,
Schryvers Anthony B.
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1997.mmi535.x
Subject(s) - transferrin , biology , mutant , haemophilus influenzae , transferrin receptor , bacterial outer membrane , permease , biochemistry , microbiology and biotechnology , ferric , gene , escherichia coli , chemistry , organic chemistry , antibiotics
Ferric‐binding proteins (FbpA) have been implicated in the transferrin receptor‐mediated iron acquisition pathways of Haemophilus influenzae and Neisseria spp. These proteins are believed to function by shuttling iron from outer membrane transferrin receptors to a specific inner membrane permease complex. However, the role of these proteins has not been conclusively resolved, as attempts at creating isogenic mutants in the fbpA genes of both species have been unsuccessful, prompting the hypothesis that FbpA may play a critical role in H . influenzae and Neisseria spp. This study describes the construction and characterization of an H . influenzae isogenic fbpA mutant. It is demonstrated that this mutant is deficient in its ability to use human transferrin as a sole iron source, even though the strain is still competent for binding human transferrin. It is also demonstrated that this mutant is impaired in its ability to use ferric citrate as an iron source, and grows at a reduced rate relative to wild type in broth supplemented with protoporphyrin rather than haemin.