The internalin proteins (inlA and inlB) of Listeria monocytogenes induce phagocytosis by normally non‐phagocytic human cells. This unique attribute makes inlA/inlB attractive as a possible therapeutic drug delivery system. inlB binds to the membrane protein “Met” present on non‐phagocytic cells and results in actin rearrangement leading to uptake of the bacterial pathogen. However, inlA binds to E‐cadherin on host epithelial cells, which mediate entry into the host cell through the recruitment of α‐catenin and β‐catenin. Either or both of these proteins may provide a means of drug delivery by conjugation of drug to the proteins. Previous work in our lab has resulted in the successful cloning and over‐expression of inlB. Current studies focus on the cloning and over‐expression of inlA and purification of native inlB. Both inlA and inlB have been partially purified with current work focused on labeling and eukaryotic uptake studies. This publication was made possible by grants from the National Center for Research Resources (5P20RR016469) and the National Institute for General Medical Science (NIGMS) (8P20GM103427), a component of the National Institutes of Health (NIH) and its contents are the sole responsibility of the authors and do not necessarily represent the official views of NIGMS or NIH.”
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