Structural insight into the dual function of LbpB in mediating Neisserial pathogenesis
Abstract
Lactoferrin-binding protein B (LbpB) is a lipoprotein present on the surface of Neisseria that has been postulated to serve dual functions during pathogenesis in both iron acquisition from lactoferrin (Lf), and in providing protection against the cationic antimicrobial peptide lactoferricin (Lfcn). While previous studies support a dual role for LbpB, exactly how these ligands interact with LbpB has remained unknown. Here, we present the structures of LbpB from N. meningitidis and N. gonorrhoeae in complex with human holo-Lf, forming a 1:1 complex and confirmed by size-exclusion chromatography small-angle X-ray scattering. LbpB consists of N- and C-lobes with the N-lobe interacting extensively with the C-lobe of Lf. Our structures provide insight into LbpB’s preference towards holo-Lf, and our mutagenesis and binding studies show that Lf and Lfcn bind independently. Our studies provide the molecular details for how LbpB serves to capture and preserve Lf in an iron-bound state for delivery to the membrane transporter LbpA for iron piracy, and as an antimicrobial peptide sink to evade host immune defenses.
Keywords
Biology (General)
Medicine
Literature (General)
Science
Immunologic diseases. Allergy
environmental sciences
social sciences
language and literature
ethnology. social and cultural anthropology
shipment of goods. delivery of goods
political institutions and public administration - asia (asian studies only)
social sciences and state - asia (asian studies only)
economic geography of the oceans (general)
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275114
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Article ID:
275114
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10.7554/eLife.71683
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Scimatic Chain (ID: 481)
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