| Title: |
A poly‐proline II helix in YadA from Yersinia enterocolitica serotype O:9 facilitates heparin binding through electrostatic interactions. |
| Authors: |
Meuskens, Ina1 (AUTHOR), Kristiansen, Per Eugen1 (AUTHOR), Bardiaux, Benjamin2 (AUTHOR), Koynarev, Vladimir Rosenov3 (AUTHOR), Hatlem, Daniel1 (AUTHOR), Prydz, Kristian1 (AUTHOR), Lund, Reidar3 (AUTHOR), Izadi‐Pruneyre, Nadia4 (AUTHOR), Linke, Dirk1 (AUTHOR) dirk.linke@ibv.uio.no |
| Source: |
FEBS Journal. Feb2024, Vol. 291 Issue 4, p761-777. 17p. |
| Subject Terms: |
*YERSINIA enterocolitica, *HEPARIN, *ELECTROSTATIC interaction, *HEPARAN sulfate, *N-terminal residues, *SULFATION |
| Abstract: |
Poly‐proline II helices are secondary structure motifs frequently found in ligand‐binding sites. They exhibit increased flexibility and solvent exposure compared to the strongly hydrogen‐bonded α‐helices or β‐strands and can therefore easily be misinterpreted as completely unstructured regions with an extremely high rotational freedom. Here, we show that the adhesin YadA of Yersinia enterocolitica serotype O:9 contains a poly‐proline II helix interaction motif in the N‐terminal region. The motif is involved in the interaction of YadAO:9 with heparin, a host glycosaminoglycan. We show that the basic residues within the N‐terminal motif of YadA are required for electrostatic interactions with the sulfate groups of heparin. Biophysical methods including CD spectroscopy, solution‐state NMR and SAXS all independently support the presence of a poly‐proline helix allowing YadAO:9 binding to the rigid heparin. Lastly, we show that host cells deficient in sulfation of heparin and heparan sulfate are not targeted by YadAO:9‐mediated adhesion. We speculate that the YadAO:9–heparin interaction plays an important and highly strain‐specific role in the pathogenicity of Yersinia enterocolitica serotype O:9. [ABSTRACT FROM AUTHOR] |
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