Adults of the parasitic nematode Dioctophyme renale locate in the renal pelvis of one (usually the right) kidney of mammals, destroying its parenchyma and function. The unaffected kidney compensates and hypertrophies such that, in most cases, there are no clear clinical signs of infection. It has recently been shown that the pseudocelomic body fluid of D. renale contains a highly abundant protein of 44 kDa in both males and females, here dubbed "dorylipophorin" (Dr-DLP-1), that binds lipids in highly apolar sites. Orthologues of this protein are specific to Clade I (Dorylaimia) of the Phylum Nematoda, initially described as the poly-cysteine and histidine-tailed proteins of unknown function of Trichinella spiralis, and one that is the immunomodulatory secreted p43 protein from Trichuris muris. We here present a biochemical and biophysical characterization of Dr-DLP-1, demonstrating that it is N-glycosylated, is more stable when bound to a fatty acid, and can be detected in the fluid surrounding the parasite in parasitized kidneys. The analysis of Dr-DLP-1 lipid binding activity showed K