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Adherence-associated lipoprotein B (AlpB) is a critical outer membrane protein and adhesin found in Helicobacter pylori, a bacterium responsible for chronic gastritis, peptic ulcers, and gastric cancer [1, 3, 8]. AlpB, along with its partner AlpA, is part of the Hop family of outer membrane proteins and is essential for the initial colonization of the human gastric mucosa [8, 31, 33]. It functions by binding to host extracellular matrix components, specifically laminin, and is a key factor in the formation of bacterial biofilms, which enhance antibiotic resistance and persistence [1, 3, 26, 30]. Because of its high conservation across H. pylori strains and its vital role in pathogenesis, AlpB is a prominent target for the development of novel anti-adhesion therapies and multi-epitope vaccines [20, 23, 33]. Experimental studies have identified several small molecules, such as allicin and curcumin, that interact with AlpB to disrupt biofilm formation, offering a potential strategy to overcome the challenges of antibiotic-resistant H. pylori infections [21]. Furthermore, AlpB is being investigated as a component of recombinant vaccines designed to elicit protective immune responses and prevent long-term colonization [20, 22, 25].
Inhibition of bacterial adhesion to host cells and disruption of biofilm formation by binding to the AlpB protein.
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