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Identification of a Streptococcus sanguis Receptor for Salivary Agglutinins

Departments of Microbiology and Biochemistry and Center for Oral Health Research, University of Pennsylvania, School of Dental Medicine, Philadelphia, Pennsylvania 19104

D. Malamud

Departments of Microbiology and Biochemistry and Center for Oral Health Research, University of Pennsylvania, School of Dental Medicine, Philadelphia, Pennsylvania 19104

B. Rosan

Departments of Microbiology and Biochemistry and Center for Oral Health Research, University of Pennsylvania, School of Dental Medicine, Philadelphia, Pennsylvania 19104

E.E. Golub

Departments of Microbiology and Biochemistry and Center for Oral Health Research, University of Pennsylvania, School of Dental Medicine, Philadelphia, Pennsylvania 19104

P. Lancy, Jr

Departments of Microbiology and Biochemistry and Center for Oral Health Research, University of Pennsylvania, School of Dental Medicine, Philadelphia, Pennsylvania 19104

The objective of this study was to characterize a fraction from oral streptococci containing receptor activity for salivary agglutinin molecules. Several species and strains of streptococci were disrupted in a Ribi press. The supernatant was nuclease-treated and subjected to differential centrifugation. Receptor activity in the fractions was measured by the inhibition of saliva-mediated bacterial aggregation. In addition, bacterial strains were tested for their ability to aggregate and to deplete saliva of agglutinin activity. Three patterns of activity were observed: Streptococcus sanguis M5 depleted saliva of agglutinin activity and aggregated well; Streptococcus sanguis CC5A depleted saliva of agglutinin but did not aggregate well; and Streptococcus faecalis S-161 neither depleted saliva of agglutinin nor did it aggregate. The 105,000 g supernatant fractions derived from Ribi-disrupted Streptococcus sanguis M5 and CC5A, but not from Streptococcus faecalis, showed dose-dependent inhibition of saliva-mediated aggregation. This inhibitory activity was non-dialyzable, had the same heat and trypsin sensitivity as that seen with intact bacteria, and was not due to enzymatic digestion of the salivary agglutinin. Iso-electric focusing revealed a single active region with a pI of 5.5 which was clearly separated from the bulk of the bacterial proteins.

Journal of Dental Research, Vol. 65, No. 2, 98-104 (1986)
DOI: 10.1177/00220345860650021901


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