Submitted on March 29, 2004
Revised on July 26, 2004
Surfactant protein D binding to terminal 
1-3 linked fucose residues and to Schistosoma mansoni
J. Koenraad van de Wetering1, Alexandra van Remoortere2, Arie B. Vaandrager1, Joseph J. Batenburg1, Lambert M.G. van Golde1, Cornelis H. Hokke2, and Jaap J. van Hellemond1*
1 Department of Biochemistry and Cell Biology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands,
2 Department of Parasitology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, The Netherlands
* To whom correspondence should be addressed. E-mail: J.vanHellemond{at}vet.uu.nl.
Pulmonary surfactant protein D (SP-D) is an important component of the innate immune system of the lung, that is thought to function by binding to specific carbohydrates on the surface of viruses and unicellular pathogens. SP-D has been shown to have a relatively high affinity for the monosaccharides mannose, glucose and fucose. However, knowledge on the SP-D binding to complex carbohydrate structures is limited and binding of SP-D to fucose in the context of an oligosaccharide has not been investigated yet. In this study we examined by surface plasmon resonance (SPR) spectroscopy the potential of SP-D to bind to various synthetic fucosylated oligosaccharides and identified Fuc
1-3GalNAc and Fuc1-3GlcNAc elements as strong ligands. These types of fucosylated glycoconjugates are presented at the surface of Schistosoma mansoni, a parasitic worm that during development transiently resides in the lung. In line with the findings by SPR, we found that SP-D can bind to larval stages of S. mansoni, demonstrating for the first time that SP-D interacts with multicellular lung pathogens.
