The agglutination of  -haemolytic streptococci by lectins

Abstract

Summary. The ability of 25 lectins, isolated from different plants and fungi, to agglutinate 95 clinical isolates of P-haemolytic streptococci was examined. Cell suspensions were untreated, trypsin-treated or boiled at pH 2.0. None of the 95 untreated cell suspensions gave a visible reaction with any of the lectins. When the cells were trypsinised, 42 strains were agglutinated with one or more lectin and after boiling at pH 2, all the strains were agglutinated. After treatment with trypsin, 20 different agglutination patterns were observed, and after boiling, 19 patterns, four of which were similar. A correlation was found between Lancefield group C and some of these patterns. Some lectins reacted specifically with group C streptococci ; DBA and WFA, both specific for D-GalNAc, DSA, a GlcNAc-specific lectin, and RPA, which showed a complex specificity, reacted only with group C strains. Furthermore, the lectin of Maackia amurensis reacted with 50 % of group B streptococci only. Agglutination assays with lectins were reproducible, easy to perform, relatively inexpensive and, therefore, applicable to studies of cell-wall structure and epidemiology of P-haemolytic streptococci.

Characterization of bovine and human group B streptococci isolated in Turkey

“…However, bovine and human GBS strains did agglutinate with lectins when the bacteria were treated with trypsin, as shown in Table 3. In agreement with our findings, Kellens et al (1993) have reported that of 95 untreated b-haemolytic streptococci, none gave a visible reaction with any of the lectins tested, whereas 42 strains agglutinated with one or more lectin when the cells were treated with trypsin. The results suggest that certain adhesins are exposed after the bacteria have been treated with trypsin.…”

“…This has often been applied to the identification and characterization of microorganisms, exploiting the specificity of binding to cell surface sugars (Ottensooser et al, 1974;Slifkin & Cumbie, 1987;Kellens et al, 1993). In the present study, none of the GBS strains agglutinated with the lectins used.…”

“…A lectin usually contains two or more binding sites for carbohydrate units; some lectins contain oligomeric structures with multiple binding sites (Ottensooser et al, 1974). Because lectins are able to bind to antibodies and thereby inhibit competitively the reaction between cellular antigen and antibody, they have been used in some typing studies (Niewerth, 1987;Slifkin & Cumbie, 1987;Kellens et al, 1993;Munoz et al, 1994).…”

T-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): Possible involvement in differential recognition of bacteria

“…Glycoconjugate agglutination test was performed by modification of the method described by Kellens et al (1993). In brief, bacterial cells were grown in three sets of 20 ml each in nutrient broth for 6 h at 37°C.…”

Lectin-Oral Streptococci Interactions

“…The extraction or enzymic treatment of streptococci may be expected to alter lectin aggregation patterns [4,[34][35][36][37][38], as streptococcal surfaces possess both hydrophobic and hydrophilic molecules [36]. Proteases might be expected to remove proteins, leaving exposed PG and group polysaccharides, while sonication would remove adventitiously bound medium components or non-c oval ently bound secreted molecules .…”