title: Identification of a glucan-binding protein C gene homologue in Streptococcus macacae.
abstract: OBJECTIVE
  The past few decades have seen the isolation of certain glucosyltransferases and a number of proteins from mutans streptococci. Some of these proteins have been shown to possess glucan-binding capabilities which confer an important virulence property on mutans streptococci for the role of these bacteria play in dental caries. Among these proteins is glucan-binding protein C, which is encoded by the gbpC gene, and which we have identified as being involved in the dextran-dependent aggregation of Streptococcus mutans. However, gbpC homologues have yet to be identified in other mutans streptococci.
  
  
  METHODS
  We carried out polymerase chain reaction amplification of Streptococcus macacae using primers that were designed based on conserved sequences of S. mutans gbpC and identified a gbpC gene homologue. The gene of that homologue was then characterized.
  
  
  RESULTS
  Nucleotide sequencing of the S. macacae gbpC homologue revealed a 1854 bp open reading frame encoding a protein with an N-terminal signal peptide. The molecular mass of the processed protein was calculated to be 67 kDa. We also found an LPxTG motif, the consensus sequence for gram-positive cocci cell wall-anchored surface proteins, which was followed by a characteristic sequence at the carboxal terminal region of the putative protein. This suggests that the S. macacae GbpC homologue protein was tethered to the cell wall.
  
  
  CONCLUSIONS
  Based on these results, together with the demonstrated glucan-binding ability of the S. macacae GbpC homologue protein, we suggest that S. macacae cells are capable of binding dextran via the GbpC homologue protein, which is similar to the S. mutans GbpC protein. In addition, Southern hybridization analysis using the S. macacae gbpC homologue as a probe showed a distribution of gbpC homologues throughout the mutans streptococci.
authors.affiliation: Department of Biochemistry, Oral Health Science Center, Tokyo Dental College, Chiba City, Japan. okamotok@tdc.ac.jp
authors.forename: K
authors.initials: K
authors.lastname: Okamoto-Shibayama
authors.forename: Y
authors.initials: Y
authors.lastname: Sato
authors.forename: Y
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: K
authors.initials: K
authors.lastname: Ohta
authors.forename: H
authors.initials: H
authors.lastname: Kizaki
mesh_terms: D020816:Amino Acid Motifs / Q000235:genetics; D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics*; D020029:Base Pairing / Q000235:genetics; D001483:Base Sequence / Q000235:genetics; D015139:Blotting, Southern; D002352:Carrier Proteins / Q000145:classification / Q000235:genetics*; D016384:Consensus Sequence / Q000235:genetics; D017124:Conserved Sequence / Q000235:genetics; D003911:Dextrans / Q000378:metabolism; D037102:Lectins / Q000145:classification / Q000235:genetics*; D008565:Membrane Proteins / Q000235:genetics*; D008970:Molecular Weight; D016366:Open Reading Frames / Q000235:genetics; D017385:Sequence Homology; D013291:Streptococcus / Q000145:classification / Q000235:genetics*; D013295:Streptococcus mutans / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D003911:Dextrans; D037102:Lectins; D008565:Membrane Proteins; C037937:glucan-binding proteins