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lüll Iron transport systems in Neisseria meningitidis Perkins-Balding D; Ratliff-Griffin M; Stojiljkovic IMicrobiol Mol Biol Rev 2004[Mar]; 68 (1): 154-71Acquisition of iron and iron complexes has long been recognized as a major determinant in the pathogenesis of Neisseria meningitidis. In this review, high-affinity iron uptake systems, which allow meningococci to utilize the human host proteins transferrin, lactoferrin, hemoglobin, and haptoglobin-hemoglobin as sources of essential iron, are described. Classic features of bacterial iron transport systems, such as regulation by the iron-responsive repressor Fur and TonB-dependent transport activity, are discussed, as well as more specific features of meningococcal iron transport. Our current understanding of how N. meningitidis acquires iron from the human host and the vaccine potentials of various components of these iron transport systems are also reviewed.|*Biological Transport[MESH]|*Gene Expression Regulation, Bacterial[MESH]|Amino Acid Sequence[MESH]|Bacterial Proteins/chemistry/genetics/*metabolism[MESH]|Humans[MESH]|Iron/*metabolism[MESH]|Molecular Sequence Data[MESH]|Neisseria meningitidis/genetics/*metabolism/pathogenicity[MESH]|Receptors, Cell Surface/chemistry/genetics/*metabolism[MESH] |