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Bacterial lactoferrin-binding protein A (LbpA) is an integral outer membrane protein found in pathogenic bacteria such as Neisseria meningitidis and Neisseria gonorrhoeae (UniProt Q51059). It serves as a TonB-dependent receptor that facilitates the acquisition of iron from human lactoferrin, a process essential for bacterial survival and proliferation within the host (PubMed: 11133477). LbpA operates as part of a bipartite receptor system alongside the surface-exposed lipoprotein LbpB. By extracting iron from host sequestering proteins, LbpA allows pathogens to overcome nutritional immunity, making it a vital virulence factor. Due to its surface exposure and essential role in metabolism, LbpA is a primary candidate for the development of recombinant vaccines and targeted antimicrobial therapies (PubMed: 25605856). However, the effectiveness of such interventions is often challenged by the high level of sequence diversity and antigenic variation observed across different clinical isolates. Research continues to focus on identifying conserved epitopes within LbpA that could provide broad-spectrum protection against various strains of Neisseria.
Binding to host lactoferrin to extract and transport ferric iron into the bacterial periplasm, essential for survival in iron-restricted host environments.
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