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Lee, Eung-Goo,Kim, Seon-Hee,Bae, Young-An,Chung, Joon-Yong,Suh, Myungkoo,Na, Byoung-Kuk,Kim, Tong-Soo,Kang, Insug,Ma, Liang,Kong, Yoon WILEY-VCH Verlag 2007 Proteomics Vol.7 No.21
<P>Parasitic organisms are incapable of de novo fatty acid synthesis due to a down-regulated expression of enzymes involved in the oxygen-dependent pathway. We investigated the uptake of host lipids by a 150-kDa hydrophobic ligand-binding protein (HLBP) of Taenia solium metacestode, an agent causative of neurocysticercosis. The protein was found to be a hetero-oligomeric complex consisting of multiple subunits (M<SUB>r</SUB> 7, 10, and 15 kDa within pH 8.0–9.7), which may originate from four unique genes of 7- and 10-kDa gene families with 2–3 polymorphic alleles/paralogs. The 15-kDa protein represented glycosylated forms of the 10-kDa. With high binding affinity to lipid analogs, these subunits evidenced high-level sequence identity with other cestode HLBPs and form a novel clade associated with excretory–secretory type HLBP. In vitro experiments with viable worms suggested that the excreted 150-kDa protein might bind to lipids, and participate in the translocation of host lipids across the syncytial membrane. This process was substantially inhibited by the specific anti-150 kDa antibodies. The protein was localized in the parasite syncytium and in the lipid droplets within host granuloma wall, where significant lipase activity was expressed. HLBP-mediated uptake of the host lipid may be critical for the parasite survival and thus could be targeted by chemotherapeutics and/or vaccine.</P>