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Jens Christian Jensenius

L-ficolin is a pattern recognition molecule specific for acetyl groups

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L-ficolin and H-ficolin are molecules of the innate immune system. Upon recognition of a suitable target they activate the complement system. The ligand recognition structure of ficolins is contained within a fibrinogen-like domain. We examined the selectivity of the ficolins through inhibiting the binding to bacteria or to beads coupled with N-acetylglucosamine. The binding of L-ficolin to Streptococcus pneumoniae 11F and the beads was inhibited by N-acetylated sugars and not by non-acetylated sugars. However, it was also inhibited by other acetylated compounds. Based on this selectivity L-ficolin is not easily defined as a lectin. The binding of H-ficolin to Aerococcus viridans was not inhibited by any of the sugars or other compounds examined. Based on the selectivity of L-ficolin we developed a new purification procedure involving affinity chromatography on N-acetylcysteine-derivatized Sepharose. The column was loaded in the presence of EDTA and high salt, and L-ficolin was eluted by decreasing the salt concentration. Further purification was achieved by ion exchange chromatography.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume279
Issue46
Pages (from-to)47513-9
Number of pages7
ISSN0021-9258
DOIs
Publication statusPublished - 2004

    Research areas

  • Acetylation, Acetylglucosamine, Amino Acid Sequence, Antigens, Bacterial, Blood Proteins, Chromatography, Affinity, Complement Activation, Humans, Lectins, Molecular Sequence Data, Protein Binding, Sequence Alignment, Streptococcaceae, Streptococcus pneumoniae, Substrate Specificity

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