Streptococcal-host interactions. Structural and functional analysis of a Streptococcus sanguis receptor for a human salivary glycoprotein - PubMed (original) (raw)
Comparative Study
. 1990 May 5;265(13):7120-6.
Affiliations
- PMID: 2185241
Free article
Comparative Study
Streptococcal-host interactions. Structural and functional analysis of a Streptococcus sanguis receptor for a human salivary glycoprotein
D R Demuth et al. J Biol Chem. 1990.
Free article
Abstract
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.
Similar articles
- Comparison of Streptococcus mutans and Streptococcus sanguis receptors for human salivary agglutinin.
Demuth DR, Lammey MS, Huck M, Lally ET, Malamud D. Demuth DR, et al. Microb Pathog. 1990 Sep;9(3):199-211. doi: 10.1016/0882-4010(90)90022-i. Microb Pathog. 1990. PMID: 1708078 - Conservation of salivary glycoprotein-interacting and human immunoglobulin G-cross-reactive domains of antigen I/II in oral streptococci.
Moisset A, Schatz N, Lepoivre Y, Amadio S, Wachsmann D, Schöller M, Klein JP. Moisset A, et al. Infect Immun. 1994 Jan;62(1):184-93. doi: 10.1128/iai.62.1.184-193.1994. Infect Immun. 1994. PMID: 8262626 Free PMC article. - Cloning and expression of a Streptococcus sanguis surface antigen that interacts with a human salivary agglutinin.
Demuth DR, Davis CA, Corner AM, Lamont RJ, Leboy PS, Malamud D. Demuth DR, et al. Infect Immun. 1988 Sep;56(9):2484-90. doi: 10.1128/iai.56.9.2484-2490.1988. Infect Immun. 1988. PMID: 3410546 Free PMC article. - Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans.
Levine MJ, Herzberg MC, Levine MS, Ellison SA, Stinson MW, Li HC, van Dyke T. Levine MJ, et al. Infect Immun. 1978 Jan;19(1):107-15. doi: 10.1128/iai.19.1.107-115.1978. Infect Immun. 1978. PMID: 415001 Free PMC article. - Platelet-streptococcal interactions in endocarditis.
Herzberg MC. Herzberg MC. Crit Rev Oral Biol Med. 1996;7(3):222-36. doi: 10.1177/10454411960070030201. Crit Rev Oral Biol Med. 1996. PMID: 8909879 Review.
Cited by
- Identification of polymorphonuclear leukocyte and HL-60 cell receptors for adhesins of Streptococcus gordonii and Actinomyces naeslundii.
Ruhl S, Cisar JO, Sandberg AL. Ruhl S, et al. Infect Immun. 2000 Nov;68(11):6346-54. doi: 10.1128/IAI.68.11.6346-6354.2000. Infect Immun. 2000. PMID: 11035744 Free PMC article. - Deletion of the central proline-rich repeat domain results in altered antigenicity and lack of surface expression of the Streptococcus mutans P1 adhesin molecule.
Brady LJ, Cvitkovitch DG, Geric CM, Addison MN, Joyce JC, Crowley PJ, Bleiweis AS. Brady LJ, et al. Infect Immun. 1998 Sep;66(9):4274-82. doi: 10.1128/IAI.66.9.4274-4282.1998. Infect Immun. 1998. PMID: 9712778 Free PMC article. - Molecular interactions of surface protein peptides of Streptococcus gordonii with human salivary components.
Hamada T, Kawashima M, Watanabe H, Tagami J, Senpuku H. Hamada T, et al. Infect Immun. 2004 Aug;72(8):4819-26. doi: 10.1128/IAI.72.8.4819-4826.2004. Infect Immun. 2004. PMID: 15271944 Free PMC article. - Complete nucleotide sequence of the gene for a surface protein antigen of Streptococcus sobrinus.
Tokuda M, Okahashi N, Takahashi I, Nakai M, Nagaoka S, Kawagoe M, Koga T. Tokuda M, et al. Infect Immun. 1991 Sep;59(9):3309-12. doi: 10.1128/iai.59.9.3309-3312.1991. Infect Immun. 1991. PMID: 1840575 Free PMC article. - Sequence and structural analysis of surface protein antigen I/II (SpaA) of Streptococcus sobrinus.
LaPolla RJ, Haron JA, Kelly CG, Taylor WR, Bohart C, Hendricks M, Pyati JP, Graff RT, Ma JK, Lehner T. LaPolla RJ, et al. Infect Immun. 1991 Aug;59(8):2677-85. doi: 10.1128/iai.59.8.2677-2685.1991. Infect Immun. 1991. PMID: 1855987 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources