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Human ficolin-2 recognition versatility extended: an update on the binding of ficolin-2 to sulfated/phosphated carbohydrates.

Authors
  • Laffly, Emmanuelle
  • Lacroix, Monique
  • Martin, Lydie
  • Vassal-Stermann, Emilie
  • Thielens, Nicole M
  • Gaboriaud, Christine
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Dec 20, 2014
Volume
588
Issue
24
Pages
4694–4700
Identifiers
DOI: 10.1016/j.febslet.2014.10.042
PMID: 25447524
Source
Medline
Keywords
License
Unknown

Abstract

Ficolin-2 has been reported to bind to DNA and heparin, but the mechanism involved has not been thoroughly investigated. X-ray studies of the ficolin-2 fibrinogen-like domain in complex with several new ligands now show that sulfate and phosphate groups are prone to bind to the S3 binding site of the protein. Composed of Arg132, Asp133, Thr136 and Lys221, the S3 site was previously shown to mainly bind N-acetyl groups. Furthermore, DNA and heparin compete for binding to ficolin-2. Mutagenesis studies reveal that Arg132, and to a lesser extent Asp133, are important for this binding property. The versatility of the S3 site in binding N-acetyl, sulfate and phosphate groups is discussed through comparisons with homologous fibrinogen-like recognition proteins.

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