Delineating the regions of human transferrin involved in interactions with transferrin binding protein B from Neisseria meningitidis

摘要: Summary Pathogenic bacteria in the Neisseriaceae possess a surface receptor mediating iron acquisition from human transferrin (hTf) that consists of transmem- brane transporter (TbpA) and surface-exposed lipoprotein (TbpB). In this study, we used hydrogen/ deuterium exchange coupled to mass spectrometry (H/DX-MS) elucidate effects on hTf by interac- tion with TbpB or derivatives TbpB. An overall conserved interaction was observed between full-length N-lobe Neisseria men- ingitidis strains B16B6 M982 represent two distinct subtypes Changes were exclusively C-lobe caused Regions localized 'lip' C1 C2 domains flank interdomain cleft sites direct contact whereas peptides within encompass binding ligands are inaccessible closed (holo) confor- mation. Although substantial domain separation upon cannot be excluded H/DX-MS data, preferred model involves conforma- tion. Alternate explanations provided for sub- stantial protection deuteration encompassing inter- but differentiated data.