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The human filarial parasite  Brugia malayi  harbors an endosymbiotic bacterium of the genus  Wolbachia . The  Wolbachia  represent an attractive target for the control of filarial induced disease as elimination of the bacteria affects molting, reproduction and survival of the worms. The molecular basis for the symbiotic relationship between  Wolbachia  and their filarial hosts has yet to be elucidated. To identify proteins involved in this process, we focused on the  Wolbachia  surface proteins (WSPs), which are known to be involved in bacteria-host interactions in other bacterial systems. Two WSP-like proteins ( w Bm0152 and  w Bm0432) were localized to various host tissues of the  B. malayi  female adult worms and are present in the excretory/secretory products of the worms. We provide evidence that both of these proteins bind specifically to  B. malayi  crude protein extracts and to individual filarial proteins to create functional complexes. The  w Bm0432 interacts with several key enzymes involved in the host glycolytic pathway, including aldolase and enolase. The  w Bm0152 interacts with the host cytoskeletal proteins actin and tubulin. We also show these interactions  in vitro  and have verified that  w Bm0432 and  B. malayi  aldolase, as well as  w Bm0152 and  B. malayi  actin, co-localize to the vacuole surrounding  Wolbachia . We propose that both WSP protein complexes interact with each other via the aldolase-actin link and/or via the possible interaction between the host's enolase and the cytoskeleton, and play a role in  Wolbachia  distribution during worm growth and embryogenesis.

plos neglected tropical diseases

A Potential Role for the Interaction of Wolbachia Surface Proteins with the Brugia malayi Glycolytic Enzymes and Cytoskeleton in Maintenance of Endosymbiosis