Flagellin -linked glycans are required for the interactions between and .

The predation and engulfment of bacteria by facilitates intimate interactions between host and prey. This process plays an important and underestimated role in the physiology, ecology and evolution of pathogenic bacteria. species can be reservoirs for many important human pathogens including is the leading cause of bacterial foodborne enteritis worldwide, despite being a microaerophile that is incapable of withstanding atmospheric levels of oxygen long-term. The persistence and transmission of this major pathogen in the natural environment outside its avian and mammalian hosts is not fully understood. Recent evidence has provided insight into the relationship of and spp. where are a transient host for this pathogen. Mutations to the flagella components were shown to affect interactions. Here, we show that the motility function of flagella is not a prerequisite for interactions and that specific -linked glycan modifications of the major flagellin, FlaA, are important for the recognition, interaction and phagocytosis by . Substitution of the -linked glycosylated serine 415 and threonine 477 with alanine within FlaA abolished interactions with and these mutants were indistinguishable from a Δ mutant. By contrast, mutation to serine 405 did not affect 11168H and interactions. Given the abundance of flagella glycosylation among clinically important pathogens, our observations may have a wider implication for understanding host-pathogen interactions.