Wbm0152, an outer membrane lipoprotein of the endosymbiont of , inhibits yeast ESCRT complex activity.

Human pathogenic filarial nematodes of the family Onchocercidae, including and cause debilitating filarial diseases such as lymphatic filariasis and river blindness. These mosquito-borne pathogens are obligately colonized by the gram-negative intracellular alphaproteobacterium, which is essential for nematode sexual reproduction, long-term survival, and pathogenicity in the mammalian host. Like many intracellular bacteria, likely uses numerous surface-exposed and secreted effector proteins to regulate its ability to persist and replicate within nematode host cells. However, due to the inability to cultivate in the laboratory and the genetic intractability of both filarial nematodes and the bacterium, the molecular underpinnings that define the bacterium:nematode relationship are almost completely unknown. In this work, we show that the expression of a outer membrane lipoprotein, Bm0152, in inhibits the activity of the conserved Endosomal Sorting Complex Required for Transport (ESCRT) complex and strongly disrupts endosomal maturation, leading to defects in ubiquitylated protein turnover. Using in vivo bimolecular fluorescence complementation, we find that Wbm0152 interacts with the Vps2p subunit of the ESCRT-III subcomplex as well as the Vps2p ortholog (BmVps2, Bm6583b) from a host nematode, . These data suggest a novel role of ESCRT in persistence providing insight into the elusive relationship between these two organisms.