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J. Biol. Chem., Vol. 265, Issue 13, 7120-7126, May, 1990
DR Demuth, EE Golub and D Malamud
Colonization of oral tissues by Streptococcus sanguis may be influenced by
a mucin-like salivary glycoprotein (SAG) through a calcium-dependent
interaction with a specific bacterial receptor. We report the nucleotide
and deduced amino acid sequence of the S. sanguis receptor (SSP-5) and show
that this protein may bind sialic acid residues of SAG. The SSP-5 protein
contains three unique structural domains, two of which consist of
repetitive amino acid sequences. The N-terminal domain is comprised of four
tandem copies of an 82-residue repeat which exhibits homology to M protein
of Streptococcus pyogenes. This region is highly charged and predicted to
be alpha-helical. A second hydrophilic repetitive domain consists of three
copies of a 39-amino acid sequence containing 30% proline flanked by
nonrepetitive proline- rich sequence. The third domain consists of 48%
proline and resides near the C terminus of the protein. Secondary structure
analysis of the SSP-5 sequence also identified four potential
helix-turn-helix motifs that resembled E-F hand calcium binding domains.
The SSP-5 protein is highly homologous to a surface antigen expressed by
the mutans streptococci and the domain structure of SSP-5 is conserved
within this family of proteins. The interactions of SSP-5 and of intact S.
sanguis with SAG were inhibited by neuraminidase digestion of the salivary
glycoprotein and by simple sugars containing sialic acid, suggesting that
sialic acid is the primary ligand involved in the binding reaction.
Streptococcal-host interactions. Structural and functional analysis of a Streptococcus sanguis receptor for a human salivary glycoprotein
Department of Biochemistry, School of Dental Medicine, University of Pennsylvania, Philadelphia 19104-6002.
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