This finding suggests that SNARE-like motifs are capable of specifically manipulating membrane fusion in a wide variety of biological environments.
Furthermore, we identified that the SNARE-like motif present in these bacterial proteins encodes the inhibitory function. More specifically, we showed that IncA and IcmG/DotF, two SNARE-like proteins respectively expressed by Chlamydia and Legionella, inhibit the endocytic SNARE machinery.
Using both an in vitro liposome fusion assay and a cellular assay, we showed that SNARE-like bacterial proteins block membrane fusion in eukaryotic cells by directly inhibiting SNARE-mediated membrane fusion. The molecular details concerning the mechanisms underlying this process are lacking. Intracellular pathogens, on the other hand, need to block fusion of their infectious phagosomes with various endocytic compartments to escape from the degradative pathway. Viruses employ glycoproteins, functionally and structurally similar to the SNARE proteins, to induce eukaryotic membrane fusion. Pathogens use diverse molecular machines to penetrate host cells and manipulate intracellular vesicular trafficking.
