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The facultative intracellular pathogen  Listeria monocytogenes  causes a severe food-borne infection in humans and animals.  L. monocytogenes  invasion factor InlB interacts with the tyrosine kinase c-Met via the N-terminal internalin domain. Previously, distinct variants of the InlB internalin domain (idInlB) have been described in  L. monocytogenes  field isolates. Three variants were used to restore full-length InlB expression in the  L. monocytogenes  strain EGDeΔ inlB . Obtained isogenic  L. monocytogenes  strains were tested in the invasion assay and intravenous, intraperitoneal, and intragastric models of infection in mice. All idInlBs were functional, restored InlB activity as an invasion factor, and improved invasion of the parental strain EGDeΔinlB into human kidney HEK23 cells. Meanwhile, distinct idInlBs provided different mortality rates and bacterial loads in internal organs. When recombinant strains were compared, the variant designated idInlB14 decreased severity of disease caused by intravenous and intraperitoneal bacterial administration, whereas this variant improved intestine colonization and stimulated intragastric infection. Obtained results demonstrated that naturally occurring idInlBs differed in their impact on severity of  L. monocytogenes  infection in mice in dependence on the infection route.

Route of Injection Affects the Impact of InlB Internalin Domain Variants on Severity ofListeria monocytogenesInfection in Mice