Blood group antigen recognition by a Streptococcus pneumoniae virulence factor

J Biol Chem. 2006 Nov 17;281(46):35263-71. doi: 10.1074/jbc.M607620200. Epub 2006 Sep 20.


The Streptococcus pneumoniae fucose utilization operon includes a gene encoding a virulence factor that belongs to family 98 in the glycoside hydrolase classification. This protein contains a C-terminal triplet of fucose binding modules that have significant amino acid sequence identity with the Anguilla anguilla fucolectin. Functional studies of these fucose binding modules reveal binding to fucosylated oligosaccharides and suggest the importance of multivalent binding. The high resolution crystal structures of ligand bound forms of one fucose binding module uncovers the molecular basis of fucose, ABH blood group antigen, and Lewisy antigen binding. These studies are extended by fluorescence microscopy to show specific binding to mouse lung tissue. These modules define a new family of carbohydrate binding modules now classified as family 47.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Blood Group Antigens / chemistry
  • Blood Group Antigens / metabolism*
  • Carbohydrate Conformation
  • Fucose / chemistry
  • Fucose / metabolism
  • Lung / metabolism
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Streptococcus pneumoniae / chemistry
  • Streptococcus pneumoniae / metabolism*
  • Streptococcus pneumoniae / pathogenicity*
  • Virulence
  • Virulence Factors / chemistry
  • Virulence Factors / metabolism*


  • Blood Group Antigens
  • Virulence Factors
  • Fucose

Associated data

  • PDB/2J1R
  • PDB/2J1S
  • PDB/2J1T
  • PDB/2J1U
  • PDB/2J1V
  • PDB/2J22