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Internalin A (InlA) is a critical surface protein of the Gram-positive bacterium Listeria monocytogenes, belonging to the internalin family characterized by leucine-rich repeat (LRR) domains. It serves as a primary ligand that mediates the attachment and entry of the pathogen into host epithelial cells by binding specifically to the host cell surface receptor E-cadherin. This interaction is essential for the bacterium to cross major physiological barriers, including the intestinal and placental barriers, which leads to systemic listeriosis. While not a target for conventional antibiotics, InlA is a significant focus for the development of novel anti-infective strategies, such as monoclonal antibodies and vaccines designed to block bacterial internalization. Understanding the structure and function of InlA and its counterparts, like Internalin B (InlB), is essential for developing targeted interventions against Listeria-mediated infections.
Inhibition of bacterial adhesion and internalization into host cells by blocking the interaction between InlA and host E-cadherin.
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