作者: Cynthia Nau Cornelissen
DOI: 10.2741/1076
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摘要: Members of the families Neisseriaceae, Pasteurellaceae and Moraxellaceae are capable transferrin-iron acquisition in absence siderophore production. They do so via expression a bi-partite receptor composed two dissimilar proteins, TbpA TbpB. Both proteins surface exposed, iron-regulated binding transferrin. However, other physiochemical, antigenic, immunogenic characteristics quite distinct. TbpB is lipoprotein, which like mammalian transferrin if discriminating between apo- holo-transferrin. Expression not essential for uptake, rare situations, gene that encodes this protein linked to encoding second component. member family TonB-dependent transporters, others accomplish ferric-siderophore vitamin B12 uptake at expense proton gradient across cytoplasmic membrane. unlike receptors where vitamins or ferric-siderophores wholly internalized, bacterial must remove iron from cell surface. This review focuses on structure-function relationships transferrin-binding their sequence antigenic diversity, mechanisms by they uptake. The contribution these pathogenesis vaccine development based also discussed.