This Article Full Text Full Text (PDF) Online Supplement All Versions of this Article: 2004-0105OCv1 31/5/565    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by van de Wetering, J. K. Articles by van Hellemond, J. J. Search for Related Content PubMed PubMed Citation Articles by van de Wetering, J. K. Articles by van Hellemond, J. J.

Surfactant Protein D Binding to Terminal 1-3–Linked Fucose Residues and to Schistosoma mansoni

Department of Biochemistry and Cell Biology, Faculty of Veterinary Medicine, Graduate School of Animal Health, Utrecht University, Utrecht; and Department of Parasitology, Center of Infectious Diseases, Leiden University Medical Center, Leiden, The Netherlands.

Address correspondence to: Dr. J. J. van Hellemond, Department of Biochemistry and Cell Biology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80176, 3508 TD, Utrecht, The Netherlands. E-mail: j.j.vanhellemond{at}vet.uu.nl

Pulmonary surfactant protein (SP)-D is an important component of the innate immune system of the lung, which 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, there is limited information on SP-D binding to complex carbohydrate structures, and binding of SP-D to fucose in the context of an oligosaccharide has not yet been investigated. In this study, we used surface plasmon resonance spectroscopy to examine the potential of SP-D to bind to various synthetic fucosylated oligosaccharides, and identified Fuc1–3GalNAc 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 surface plasmon resonance, 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.

Abbreviations: bronchoalveolar lavage, BAL • bovine serum albumin, BSA • carbohydrate recognition domain, CRD • ethylenediaminetetraacetic acid, EDTA • fluorescein isothiocyanate, FITC • Fuc1–2Fuc1–3GlcNAc, FF-Gn • Fuc1–3GlcNAc, F-Gn • Fuc1–3GalNAcß1–4GlcNAc, F-LDN • GlcNAc, Gn • human serum albumin, HSA • HEPES-buffered saline, HBS • immunoglobulin, Ig • GalNAcß1–4GlcNAc, LDN • lNAcß1–4(Fuc1–3)GlcNAc, LDN-F • Galß1–4(Fuc1–3)GlcNAc, Lewis-X • mannan-binding lectin, MBL • phosphate-buffered saline, PBS • polyvinylidene fluoride, PVDF • sodium dodecyl sulfate–polyacrylamide gel electrophoresis, SDS-PAGE • surfactant protein, SP • surface plasmon resonance, SPR • Tris-buffered saline and Tween, TBS-T