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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-F4EA-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-BE5F-A
Genre: Journal Article

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 Creators:
Reinhardt, Anika1, Author              
Wehle, Marko2, Author              
Geißner, Andreas1, Author              
Crouch, Erika C., Author
Kang, Yu2, Author              
Yang, You3, Author              
Chakkumkal, Anish1, Author              
Santer, Mark2, Author              
Seeberger, Peter H.4, Author              
Affiliations:
1Chakkumal Anish, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863299              
2Mark Santer, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863326              
3Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863306              
4Peter H. Seeberger, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2040285              

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Free keywords: surfactant protein D; D324N+D325N+R343K mutant; carbohydrate recognition domain; lipopolysaccharide inner core structure; Gramnegative bacteria; glycan array; surface plasmon resonance; molecular docking; molecular dynamics simulations; synthetic glycans
 Abstract: 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.

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 Dates: 2016-06-252016-09
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1016/j.jsb.2016.06.019
BibTex Citekey: Reinhardt2016
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Title: Journal of Structural Biology
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 195 (3) Sequence Number: - Start / End Page: 387 - 395 Identifier: ISSN: 1047-8477