To better understand how IncE can recruit the SNX5-containing SNX-BAR complexes to inclusion membranes we constructed an in silico model of the SNX5-SNX1 heterodimeric PX-BAR proteins (Figure 7B). Consistent with the length of the IncE C-terminal cytoplasmic sequence the model predicts that the IncE sequence will bind to the surface of SNX5 close to, but oriented away from, the inclusion membrane. While PX domains are commonly able to recognise PtdIns3P lipid headgroups, SNX5-related proteins lack the typical binding pocket (Figure 7B right panel), and there is some controversy regarding their ability to mediate specific membrane interactions (Koharudin et al., 2009; Teasdale and Collins, 2012). We propose that in the context of C. trachomatis infection, SNX5-related proteins are directly associated with the inclusion via IncE protein-protein interactions in a phosphoinositide-independent manner, and are able to recruit their heterodimeric partners SNX1 and SNX2 (Sierecki et al., 2014; van Weering et al., 2012; Wassmer et al., 2009). The PX-BAR-domain containing complexes are then localised to the inclusion in a retromer-independent manner (Mirrashidi et al., 2015), and may contribute to the formation of the dynamic inclusion-associated membrane tubules.