Crystal structures of human SP-D complexed with synthetic oligosaccharides suggest a role for phosphorylated inner core LPS saccharides in host-pathogen interactions (2025)
Preprint / Working Paper
Williams, H. M., Watson, A., Madsen, J., Clark, H. W., Hood, D. W., Oscarson, S., Greenhough, T. J., & Shrive, A. K. (2025). Crystal structures of human SP-D complexed with synthetic oligosaccharides suggest a role for phosphorylated inner core LPS saccharides in host-pathogen interactions

The innate immune protein human surfactant protein D (SP-D) recognises pathogens in the lungs via binding to carbohydrate surface structures. SP-D has been shown to target gram-negative bacterial lipopolysaccharide via calcium-dependent binding, pref... Read More about Crystal structures of human SP-D complexed with synthetic oligosaccharides suggest a role for phosphorylated inner core LPS saccharides in host-pathogen interactions.

Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs (2023)
Journal Article
Williams, H. M., Moeller, J. B., Burns, I., Schlosser, A., Sorensen, G. L., Greenhough, T. J., Holmskov, U., & Shrive, A. K. (2023). Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs. Journal of Biological Chemistry, 105552. https://doi.org/10.1016/j.jbc.2023.105552

Fibrinogen C-domain containing-1 (FIBCD1) is an immune protein proposed to be involved in host recognition of chitin on the surface of pathogens. As FIBCD1 readily binds to acetylated molecules, we have determined the high-resolution crystal structur... Read More about Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs.