Link to Pubmed [PMID] – 29666193
J. Biol. Chem. 2018 Jun;293(24):9265-9276
() is a facultative intracellular bacterial pathogen and the causative agent of listeriosis, a rare but fatal disease. During infection, can traverse several physiological barriers; it can cross the intestine and placenta barrier and, in immunocompromised individuals, the blood-brain barrier. With the recent plethora of sequenced genomes available for , it is clear that the complete repertoire of genes used by to interact with its host remains to be fully explored. Recently, we focused on secreted proteins because they are likely to interact with host cell components. Here, we investigated a putatively secreted protein of , Lmo1656, that is present in most sequenced strains of but absent in the nonpathogenic species gene is predicted to encode a small, positively charged protein. We show that Lmo1656 is secreted by Furthermore, deletion of the gene (Δ) attenuates virulence in mice infected orally but not intravenously, suggesting that Lmo1656 plays a role during oral listeriosis. We identified sorting nexin 6 (SNX6), an endosomal sorting component and BAR domain-containing protein, as a host cell interactor of Lmol656. SNX6 colocalizes with WT during the early steps of infection. This colocalization depends on Lmo1656, and RNAi of SNX6 impairs infection in infected tissue culture cells, suggesting that SNX6 is utilized by during infection. Our results reveal that Lmo1656 is a novel secreted virulence factor of that facilitates recruitment of a specific member of the sorting nexin family in the mammalian host.