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

23 December 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


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.


Surface Plasmon Resonance
Molecular dynamics simulations
H1, H1 transfer NOESY NMR
Shigella flexneri O-antigen
Bacteriophage tailspike proteins
Carbohydrate-Binding Proteins


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