Abstract: Methods for selectively detecting a live pathogen in a sample containing live and dead pathogens, without detecting the dead pathogen are disclosed. Such methods may include: (i) immobilizing at least a portion of the live and dead pathogens on a solid support with a physical barrier; (ii) incubating the solid support in a growth medium, where the live pathogen can multiply and the multiplied pathogen move from the solid support to a supernatant of the growth medium; and (iii) detecting the multiplied pathogen in the supernatant by a pathogen assay.

Abstract: The present disclosure relates to the isolation of a novel reagent selected for its binding characteristics to the proteins internalin B or internalin A. InIB is a surface-localized protein of Listeria monocytogenes that binds and activates the receptor tyrosine kinase Met. InIB promotes invasion of a number of cells including hepatocytes, endothelial and epithelial cell lines and causes activation of the actin-mediated internalization of the bacterium. InIA belongs to a large group of surface-localized leucine-rich repeat (LRR) proteins identified in the Listeria genome. InIA enables Listeria monocytogenes to invade non-phagocytic cells such as those of the human intestinal epithelium and is sufficient for adhesion to and inducing uptake into epithelial cells.

Abstract: Aptamers bind to Listeria surface proteins. A method of assaying a sample for the presence of Listeria monocytogenes includes exposing the sample to an aptamer that specifically binds one of the following proteins: Listeria monocytogenes internalin A protein, Listeria monocytogenes internalin E protein, and Listeria monocytogenes 0610 protein. The presence of Listeria monocytogenes in the sample is detected when the aptamer binds the protein present in the sample. A method of treating Listeria monocytogenes infection includes administering the aptamers to the mammal at a concentration sufficient to reduce Listeria monocytogenes infection.

Abstract: The present disclosure relates to the isolation of a novel reagent selected for its binding characteristics to the proteins internalin B or internalin A. InIB is a surface-localized protein of Listeria monocytogenes that binds and activates the receptor tyrosine kinase Met. InIB promotes invasion of a number of cells including hepatocytes, endothelial and epithelial cell lines and causes activation of the actin-mediated internalization of the bacterium. InIA belongs to a large group of surface-localized leucine-rich repeat (LRR) proteins identified in the Listeria genome. InIA enables Listeria monocytogenes to invade non-phagocytic cells such as those of the human intestinal epithelium and is sufficient for adhesion to and inducing uptake into epithelial cells.

Abstract: Aptamers bind to Listeria surface proteins. A method of assaying a sample for the presence of Listeria monocytogenes includes exposing the sample to an aptamer that specifically binds one of the following proteins: Listeria monocytogenes internalin A protein, Listeria monocytogenes internalin E protein, and Listeria monocytogenes 0610 protein. The presence of Listeria monocytogenes in the sample is detected when the aptamer binds the protein present in the sample. A method of treating Listeria monocytogenes infection includes administering the aptamers to the mammal at a concentration sufficient to reduce Listeria monocytogenes infection.