Anchor peptide of transferrin-binding protein B is required for interaction with transferrin-binding protein A |
| |
Authors: | Yang Xue Yu Rong-hua Calmettes Charles Moraes Trevor F Schryvers Anthony B |
| |
Affiliation: | Department of Microbiology and Infectious Diseases, University of Calgary, Calgary T2N 4N1 Alberta, Canada. |
| |
Abstract: | Gram-negative bacterial pathogens belonging to the Pasteurellaceae, Moraxellaceae, and Neisseriaceae families rely on an iron acquisition system that acquires iron directly from host transferrin (Tf). The process is mediated by a surface receptor composed of transferrin-binding proteins A and B (TbpA and TbpB). TbpA is an integral outer membrane protein that functions as a gated channel for the passage of iron into the periplasm. TbpB is a surface-exposed lipoprotein that facilitates the iron uptake process. In this study, we demonstrate that the region encompassing amino acids 7-40 of Actinobacillus pleuropneumoniae TbpB is required for forming a complex with TbpA and that the formation of the complex requires the presence of porcine Tf. These results are consistent with a model in which TbpB is responsible for the initial capture of iron-loaded Tf and subsequently interacts with TbpA through the anchor peptide. We propose that TonB binding to TbpA initiates the formation of the TbpB-TbpA complex and transfer of Tf to TbpA. |
| |
Keywords: | Bacteria Iron Membrane Receptors Transport Metals Gram-negative Outer Membrane Pathogen Surface Receptor Transferrin |
本文献已被 PubMed 等数据库收录! |