FLK-2100 Search Results


94
Vector Laboratories fluorescein labeled lectin
( A ) Binding of plant lectins to surface structures of capsule-deficient S. suis strains (ΔCPS). SBA binds to N -acetylgalactosamine (GalNAc) and, to a lesser extent, galactose (Gal); RCA 120 binds to both Gal and GalNAc; sWGA has a special affinity to N -acetylglucosamine (GlcNAc). Data from biological triplicates are presented as mean values ± SD. ( B ) Glycosyl composition analysis by GC-MS of TMS (trimethylsilyl) derivatives of methyl glycosides of S. suis RPS from S10 and 861160 released by mild acid hydrolysis after chemical N -acetylation. ( C ) Plant <t>lectin</t> binding to isolated RPS from S. suis S10 and 861160. Data show technical triplicates (mean values ± SD) and are representative for two independent experiments. ( D and E ) Presence and absence of the most abundant glycosyl linkage residues (D) and phosphate (E) of S. suis RPS from S10 and 861160. Glycosyl linkage residues were analyzed by GC-MS of partially methylated alditol acetate derivatives. Phosphate was determined by malachite green assay following hydrolysis with hydrochloric acid and digestion with alkaline phosphatase. Original data is in tables S2 and S3.
Fluorescein Labeled Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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( A ) Binding of plant lectins to surface structures of capsule-deficient S. suis strains (ΔCPS). SBA binds to N -acetylgalactosamine (GalNAc) and, to a lesser extent, galactose (Gal); RCA 120 binds to both Gal and GalNAc; sWGA has a special affinity to N -acetylglucosamine (GlcNAc). Data from biological triplicates are presented as mean values ± SD. ( B ) Glycosyl composition analysis by GC-MS of TMS (trimethylsilyl) derivatives of methyl glycosides of S. suis RPS from S10 and 861160 released by mild acid hydrolysis after chemical N -acetylation. ( C ) Plant lectin binding to isolated RPS from S. suis S10 and 861160. Data show technical triplicates (mean values ± SD) and are representative for two independent experiments. ( D and E ) Presence and absence of the most abundant glycosyl linkage residues (D) and phosphate (E) of S. suis RPS from S10 and 861160. Glycosyl linkage residues were analyzed by GC-MS of partially methylated alditol acetate derivatives. Phosphate was determined by malachite green assay following hydrolysis with hydrochloric acid and digestion with alkaline phosphatase. Original data is in tables S2 and S3.

Journal: Science Advances

Article Title: A conserved glycan motif induces broadly reactive functional antibodies against the zoonotic pathogen Streptococcus suis

doi: 10.1126/sciadv.adz1854

Figure Lengend Snippet: ( A ) Binding of plant lectins to surface structures of capsule-deficient S. suis strains (ΔCPS). SBA binds to N -acetylgalactosamine (GalNAc) and, to a lesser extent, galactose (Gal); RCA 120 binds to both Gal and GalNAc; sWGA has a special affinity to N -acetylglucosamine (GlcNAc). Data from biological triplicates are presented as mean values ± SD. ( B ) Glycosyl composition analysis by GC-MS of TMS (trimethylsilyl) derivatives of methyl glycosides of S. suis RPS from S10 and 861160 released by mild acid hydrolysis after chemical N -acetylation. ( C ) Plant lectin binding to isolated RPS from S. suis S10 and 861160. Data show technical triplicates (mean values ± SD) and are representative for two independent experiments. ( D and E ) Presence and absence of the most abundant glycosyl linkage residues (D) and phosphate (E) of S. suis RPS from S10 and 861160. Glycosyl linkage residues were analyzed by GC-MS of partially methylated alditol acetate derivatives. Phosphate was determined by malachite green assay following hydrolysis with hydrochloric acid and digestion with alkaline phosphatase. Original data is in tables S2 and S3.

Article Snippet: Subsequently, 12.5 μl of bacterial suspension was incubated in a 96-well V-bottom plate with the same volume of pig serum or fluorescein-labeled lectin (Vector Laboratories, FLK-2100 and FL-1021S-5).

Techniques: Binding Assay, Gas Chromatography-Mass Spectrometry, Isolation, Methylation, Malachite Green Assay