Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Bacterial iron transport is critical for growth of pathogens in the host environment, where iron is limited as a form of nonspecific immunity. For Gram-negative bacteria such as Haemophilus influenzae, iron first must be transported across the outer membrane and into the periplasmic space, then from the periplasm to the cytosol. H. influenzae express a periplasmic iron-binding protein encoded by the hitA gene. This gene is organized as the first of a three-gene operon purported to encode a classic high affinity iron acquisition system that includes hitA, a cytoplasmic permease (hitB), and a nucleotide binding protein (hitC). In this study we describe the cloning, overexpression, and purification of the H. influenzae hitA gene product. The function of this protein is unambiguously assigned by demonstrating its ability to compete for iron bound to the chemical iron chelator 2,2'-dipyridyl, both in vitro and within the periplasmic space of a siderophore-deficient strain of Escherichia coli. Finally, the importance of a functional hitABC operon for iron acquisition is demonstrated by complementation of this siderophore-deficient E. coli to growth on dipyridyl-containing medium. These studies represent a detailed genetic, biochemical, and physiologic description of an active transport system that has evolved to efficiently transport iron and consequently is widely distributed among Gram-negative pathogenic bacteria.
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PMID:Biochemical characterization of a Haemophilus influenzae periplasmic iron transport operon. 755 48

The ferric binding protein (FbpA) is one of the major proteins regulated by the level of environmental iron in the genus Neisseria. Its conservation in all species of pathogenic Neisseria has been demonstrated, and the possible role that it plays in the iron uptake mechanisms in these bacteria has been postulated. Similar proteins in Haemophilus influenzae (HitA) and in Serratia marcescens (SfuA) have been described, but relationships with the meningococcal FbpA could not be proven. Although supposedly periplasmic, the exact location of FbpA remains controversial because some molecules, or parts of them, have been found exposed to the bacterial outer surface. The DNA sequence downstream of the fbpA gene has been recently analysed, finding an operon composed of three open reading frames: fbpA, encoding for FbpA; fbpB, that codifies a cytoplasmic permease, and fbpC, that contains the information for a nucleotide binding protein. These proteins would form an iron transport system through the periplasmic space. FbpA is highly antigenic in mice when injected in purified form, shows intraspecies and interspecies antigenic homogenicity, and specific anti-FbpA antibodies are fully cross-reactive; nevertheless, the in vivo induction of anti-FbpA antibodies in man is still polemical. Recent studies reveal that the purified FbpA induces a fair response of bactericidal antibodies in mice.
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PMID:The neisserial 37 kDa ferric binding protein (FbpA). 1042 7