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Structure binding relationship of human surfactant protein D and various lipopolysaccharide inner core structures

MPG-Autoren
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Reinhardt,  Anika
Chakkumal Anish, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Wehle,  Marko
Mark Santer, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Geißner,  Andreas
Chakkumal Anish, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Kang,  Yu
Mark Santer, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Yang,  You
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Chakkumkal,  Anish
Chakkumal Anish, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Santer,  Mark
Mark Santer, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Seeberger,  Peter H.
Peter H. Seeberger, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Zitation

Reinhardt, A., Wehle, M., Geißner, A., Crouch, E. C., Kang, Y., Yang, Y., et al. (2016). Structure binding relationship of human surfactant protein D and various lipopolysaccharide inner core structures. Journal of Structural Biology, 195(3), 387-395. doi:10.1016/j.jsb.2016.06.019.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002A-F4EA-3
Zusammenfassung
As a major player of the innate immune system, surfactant protein D (SP-D) recognizes and promotes elimination of various pathogens such as Gram-negative bacteria. SP-D binds to l-glycero-d-manno-heptose (Hep), a constituent of the partially conserved lipopolysaccharide (LPS) inner core of many Gram-negative bacteria. Binding and affinity of trimeric human SP-D to Hep in distinct \LPS\} inner core glycans differing in linkages and adjacent residues was elucidated using glycan array and surface plasmon resonance measurements that were compared to in silico interaction studies. The combination of in vitro assays using defined glycans and molecular docking and dynamic simulation approaches provides insights into the interaction of trimeric SP-D with those glycan ligands. Trimeric SP-D wildtype recognized larger \{LPS\} inner core oligosaccharides with slightly enhanced affinity than smaller compounds suggesting the involvement of stabilizing secondary interactions. A trimeric human SP-D mutant D324N+D325N+R343K resembling rat SP-D bound to various \{LPS\} inner core structures in a similar pattern as observed for the wildtype but with higher affinity. The selective mutation of SP-D promotes targeting of \{LPS\ inner core oligosaccharides on Gram-negative bacteria to develop novel therapeutic agents.