Agglutination of Streptococcus mutans by low-molecular-weight salivary components: effect of beta 2-microglobulin

Abstract

Radiolabeled monomeric human 02-microglobulin (0i2m) was tested for binding to Streptococcus mutans strains in buffers containing I mM calcium (Ca2+). Binding was seen to strains with a previously established binding capacity of aggregated 12m. Monomeric P2m agglutinated 012m-binding strains when Ca`was present. At Ca2+ concentrations of 1.4 mM, 0.032 jig of monomeric 132m per ml caused bacterial agglutination.

Antimicrobial peptides of the oral cavity

“…However, this difference was not noted in a study of juvenile periodontitis saliva, where the beta‐2‐microglobulin level did not differ between patients and controls, while serum levels were higher in periodontitis patients than in controls (5). Beta‐2‐microglobulin causes agglutination of S. mutans in the presence of 1.4 m m Ca 2+ (66).…”

Binding of Salivary Glycoprotein-Secretory Immunoglobulin A Complex to the Surface Protein Antigen of Streptococcus mutans

“…Various salivary components, such as secretory immunoglobulin A (sIgA) (36), ␤ 2 -microglobulin (12), histidine-rich polypeptides (32), a 60-kDa glycoprotein (1), lysozyme (39), lactoferrin (43), and high-molecular-mass glycoproteins (4,7,13,20), have been reported to bind to S. mutans and/or to induce agglutination of the organism. Much attention has also been focused on the interaction between PAc and salivary components (5,8,21,(27)(28)(29).…”