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Parasitic nematodes produce an unusual class of fatty acid and retinol (FAR)-binding proteins that may scavenge host fatty acids and retinoids. Two FARs from  Brugia malayi  ( Bm- FAR-1 and  Bm- FAR-2) were expressed as recombinant proteins, and their ligand binding, structural characteristics, and immunogenicities examined. Circular dichroism showed that r Bm -FAR-1 and r Bm -FAR-2 are similarly rich in α-helix structure. Unexpectedly, however, their lipid binding activities were found to be readily differentiated. Both FARs bound retinol and  cis- parinaric acid similarly, but, while r Bm -FAR-1 induced a dramatic increase in fluorescence emission and blue shift in peak emission by the fluorophore-tagged fatty acid (dansyl-undecanoic acid), r Bm -FAR-2 did not. Recombinant forms of the related proteins from  Onchocerca volvulus , r Ov -FAR-1 and r Ov -FAR-2, were found to be similarly distinguishable. This is the first FAR-2 protein from parasitic nematodes that is being characterized. The relative protein abundance of  Bm -FAR-1 was higher than  Bm- FAR-2 in the lysates of different developmental stages of  B .  malayi . Both FAR proteins were targets of strong IgG1, IgG3 and IgE antibody in infected individuals and individuals who were classified as endemic normal or putatively immune. In a  B .  malayi  infection model in gerbils, immunization with r Bm- FAR-1 and r Bm -FAR-2 formulated in a water-in-oil-emulsion (®Montanide-720) or alum elicited high titers of antigen-specific IgG, but only gerbils immunized with r Bm -FAR-1 formulated with the former produced a statistically significant reduction in adult worms (68%) following challenge with  B .  malayi  infective larvae. These results suggest that FAR proteins may play important roles in the survival of filarial nematodes in the host, and represent potential candidates for vaccine development against lymphatic filariasis and related filarial infections.

plos neglected tropical diseases

Ligand binding properties of two Brugia malayi fatty acid and retinol (FAR) binding proteins and their vaccine efficacies against challenge infection in gerbils