Two recent studies have greatly expanded the repertoire of host cell proteins known to associate with chlamydial inclusions and Inc proteins (Aeberhard et al., 2015; Mirrashidi et al., 2015). Both reports confirmed that membrane trafficking proteins are major components of the inclusion proteome; and in particular members of the endosomal sorting nexin (SNX) family are highly enriched. Specifically it was shown that the C. trachomatis IncE/CT116 protein could recruit SNX proteins containing bin-amphiphysin-Rvs (BAR) domains SNX1, SNX2, SNX5 and SNX6 (Mirrashidi et al., 2015). SNX1 and SNX2 are highly homologous and form heterodimeric assemblies with either SNX5 or SNX6 to promote endosomal membrane tubulation and trafficking (van Weering et al., 2012). A fifth protein SNX32 is highly similar to SNX5 and SNX6 but is almost exclusively expressed in the brain and has not yet been characterized. SNX recruitment to the inclusion occurs via the C-terminal region of IncE interacting with the phox-homology (PX) domains of SNX5 or SNX6 (Mirrashidi et al., 2015) (Figure 1A). Interestingly, RNAi-mediated depletion of SNX5/SNX6 does not slow infection but rather increases the production of infectious C. trachomatis progeny suggesting that the SNX recruitment is not done to enable bacterial infection. Instead it was proposed that because SNX proteins regulate endocytic and lysosomal degradation, the manipulation by IncE could be an attempt to circumvent SNX-enhanced bacterial destruction (Aeberhard et al., 2015; Mirrashidi et al., 2015).