Listeria monocytogenes cell-surface receptors (Inl)

Listeria monocytogenes cell-surface receptors, primarily the internalin family (InlA, InlB), are critical bacterial proteins that mediate the attachment and internalization of the pathogen into host cells (1.2.1, 1.2.5). Internalin A (InlA) specifically interacts with host E-cadherin, facilitating entry into epithelial cells, while Internalin B (InlB) binds to the Met receptor (hepatocyte growth factor receptor) to promote entry into a wider range of cell types, including hepatocytes and endothelial cells (1.2.3, 1.2.4). These surface proteins are essential for the bacterium to cross physiological barriers, such as the intestinal, blood-brain, and placental barriers, leading to severe infections like listeriosis (1.2.2, 1.3.5). While traditional treatment for listeriosis involves antibiotics like ampicillin and gentamicin, these surface receptors are significant targets for the development of novel therapeutics, including monoclonal antibodies and antisense oligonucleotides designed to block bacterial entry (1.1.1, 1.1.3). Understanding the structural basis of these interactions is vital for designing inhibitors that can prevent the systemic spread of the infection (1.3.3, 1.3.4).

Other names

Internalin proteinsInternalin A (InlA)Internalin B (InlB)Listeria surface invasinsListeria adhesinsListeria monocytogenes surface proteins

Inhibition of bacterial attachment and entry into host cells by blocking the interaction between bacterial internalins and host cell receptors such as E-cadherin and the Met receptor (1.1.2, 1.2.3).