Abstract
Transferrin receptors serve as critical iron acquisition systems in several species of Proteobacteria. Histophilus somni, a pathogen of cattle and sheep and an occasional commensal of goats, is unique in encoding two transferrin receptor systems: a bipartite receptor containing TbpA and TbpB and a monopartite system consisting of TbpA2. Pogoutse and Moraes (e00177-20) measured the binding of each Tbp to a range of transferrins from several different species and showed that H. somni TbpA, TbpB, and TbpA2 display different levels of selectivity. The more promiscuous TbpA2 and TbpB may contribute to H. somni’s ability to infect sheep and goats, expanding its host range.
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