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Sökning: WFRF:(Blixt Martin) > Lunds universitet

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1.
  • Goel, Suchi, et al. (författare)
  • RIFINs are adhesins implicated in severe Plasmodium falciparum malaria
  • 2015
  • Ingår i: Nature Medicine. - : Springer Science and Business Media LLC. - 1078-8956 .- 1546-170X. ; 21:4, s. 314-317
  • Tidskriftsartikel (refereegranskat)abstract
    • Rosetting is a virulent Plasmodium falciparum phenomenon associated with severe malaria. Here we demonstrate that P. falciparum-encoded repetitive interspersed families of polypeptides (RIFINs) are expressed on the surface of infected red blood cells (iRBCs), bind to RBCs-preferentially of blood group A-to form large rosettes and mediate microvascular binding of iRBCs. We suggest that RIFINs have a fundamental role in the development of severe malaria and thereby contribute to the varying global distribution of ABO blood groups in the human population.
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2.
  • Tobola, Felix, et al. (författare)
  • Engineering the Ligand Specificity of the Human Galectin-1 by Incorporation of Tryptophan Analogues
  • 2022
  • Ingår i: ChemBioChem. - : Wiley. - 1439-4227 .- 1439-7633. ; 23:5
  • Tidskriftsartikel (refereegranskat)abstract
    • Galectin-1 is a β-galactoside-binding lectin with manifold biological functions. A single tryptophan residue (W68) in its carbohydrate binding site plays a major role in ligand binding and is highly conserved among galectins. To fine tune galectin-1 specificity, we introduced several non-canonical tryptophan analogues at this position of human galectin-1 and analyzed the resulting variants using glycan microarrays. Two variants containing 7-azatryptophan and 7-fluorotryptophan showed a reduced affinity for 3’-sulfated oligosaccharides. Their interaction with different ligands was further analyzed by fluorescence polarization competition assay. Using molecular modeling we provide structural clues that the change in affinities comes from modulated interactions and solvation patterns. Thus, we show that the introduction of subtle atomic mutations in the ligand binding site of galectin-1 is an attractive approach for fine-tuning its interactions with different ligands.
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