Although more than fifty putative Incs have been identified in C. trachomatis, the exact roles of these inclusion membrane proteins are still poorly understood. Chlamydiae manipulate the host cellular and signaling networks via interactions between the cytoplasmic region of Incs and numerous host cell proteins. Recent studies reported retrograde trafficking proteins as significant components of the inclusion, with sorting nexin family members being particularly enriched (Aeberhard et al., 2015; Mirrashidi et al., 2015). In this study, we present the first reported crystal structure of a chlamydial inclusion protein (IncE) binding to its host effector protein (SNX5). While the detailed mechanism of IncE-mediated protein recruitment will be specific to this family member, the principle of extended cytoplasmic Inc sequences engaging with cellular host proteins on the inclusion is certain to be a general one. A simple analogy would be to consider the Inc proteins as being like a molecular ‘velcro’ that recognises and attaches host machinery needed for bacterial replication and survival.