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Bdellovibrio bacteriovorus is a bacterium that preys on other Gram-negative bacteria. These predatory bacteria attach to and invade the periplasm of their prey and consume them from within.
Following intraperiplasmic cell division B. bacteriovorus progeny are released to complete the predatory life cycle. Before invasion, B. bacteriovorus must recognize and adhere to its prey,
followed by traversal through layers of prey lipopolysaccharide and peptidoglycan. However, the mechanisms underlying prey recognition and invasion of their bacterial hosts are elusive. In
this new study, Caulton, Lambert, Tyson et al. describe trimeric fibre proteins with diverse adhesive tips that enable the identification of a broad range of prey.
The authors went on to characterize the MAT proteins and found that some contained a phage-like autoproteolytic S74 protease and chaperone domain. The authors thus grouped the MAT proteins
into two subfamilies, S74 and non-S74 (NS74). On the basis of their results, the authors hypothesized that the two subfamilies represent adhesins with diverse adhesive tips.
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