These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
Sf6TSP_Cys_draft_191219_archive.pdf (3.47 MB)

Increasing the Affinity of an O-Antigen Polysaccharide Binding Site in Shigella Flexneri Bacteriophage Sf6 Tailspike Protein

submitted on 19.12.2019, 18:05 and posted on 23.12.2019, 21:01 by R. Sonja Kunstmann, Olof Engström, Marko Wehle, Göran Widmalm, Mark Santer, Stefanie Barbirz
We analysed the tailspike from bacteriophage Sf6 in complex with the O-polysaccharide of the pathogen Shigella flexneri. The conformational space populated by the polyrhamnose backbone of the S. flexneri O-polysaccharide as studied by an octasaccharide in complex with Sf6TSP could be well described with 2D 1H,1H-trNOESY NMR, utilizing a combination of methine-methine and methine-methyl correlations. The results are in good agreement with the conformations obtained from molecular dynamics (MD) simulations. To examine the impact of amino acid exchanges in the glycan binding site of Sf6TSP, MD simulations were used to predict increased O-polysaccharide binding affinities. We used surface plasmon resonance on S. flexneri O-polysaccharide surfaces to measure affinity increases in the obtained mutants.


International Max Planck Research School on Multiscale Biosystems

European Union's Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie grant agreement no. 713683 (COFUNDfellowsDTU)

Swedish Research Council (no. 2017-03703)

Knut and Alice Wallenberg Foundation

Deutsche Forschungsgemeinschaft (BA4046/1-2)


Email Address of Submitting Author


Department of Biotechnology and Biomedicine, Technical University of Denmark



ORCID For Submitting Author


Declaration of Conflict of Interest

The authors declare no competing interests.