A great paper from the University of Heidelberg, recently published in Frontiers in Immunology, showed that T2R38 may function in human neutrophils as a sensor for N-(3-oxododecanoyl)-L-homoserine lactone (C12HSL), a quorum-sensing molecule used by Pseudomonas aeruginosa and other gram-negative bacteria. Neutrophils, the most abundant type of white blood cell, are "first responders" that act during the early phases of inflammation to phagocytose (ingest) invading microbes as well as release antimicrobial compounds.
This paper (Maurer, et al. "Tasting Pseudomonas aeruginosa biofilms: human neutrophils express the bitter receptor T2R38 as a sensor for the quorum sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone") can be accessed for free here.
This study, in addition to introducing another cell type in which T2R38 functions in an immune role, confirms what we published in 2012 in JCI, namely that T2R38 functions as an inter-kingdom protein sensor for eukaryotic cells to detect bacterial acyl-homoserine lactones. We're very happy to see more research supporting an important role for taste receptors in human innate immunity.