Disease relevance of BF3936

• Sialidase activity was detected in 94% of 66 isolates from the Bacteroides fragilis group, 98% of 66 B. bivius isolates, and all isolates of the following species (number of isolates follows species name): B. capillosus, 4; B. levii, 2; B. denticola, 22; B. loescheii, 23; B. melaninogenicus, 32; B. forsythus, 44; and B. buccalis, 2 [1].
• Of 28 specimens from women with bacterial vaginosis, 27 (96%) yielded sialidase-positive bacteria, at a median concentration of 10(6.5) CFU/ml of vaginal fluid [2].
• These data demonstrate sialidase activity in several species of the genera Bacteroides and Porphyromonas and suggest that this characteristic may be useful for identification [1].
• These data suggest that vaginal fluid sialidase is highly correlated with bacterial vaginosis and that the probable sources for this enzyme activity are the Bacteroides and Prevotella species present in the vagina [2].
• Sialidase activity was found in 10 (100%) of 10 isolates of Capnocytophaga ochracea of C. sputigena but not in any of 4 C. gingivalis isolates [1].

High impact information on BF3936

• The N-terminal amino acid sequence of this sialidase, Ala-Asp-X-Ile-Phe-Val-Arg-Glu-Thr-Arg-Ile-Pro-, was determined [3].
• A sialidase from Bacteroides fragilis SBT3182 was purified 2,240-fold to apparent homogeneity by ammonium sulfate precipitation and sequential chromatographies on DEAE-Toyopearl 650M, Hydroxyapatite, MonoS and Superose6 columns [3].
• A rapid assay of the sialidase activity in species of the Bacteroides fragilis group by using peanut lectin hemagglutination [4].
• Sialidase activity, a virulence determinant, was associated with these sub-cellular structures in all the strains, but in an inverse relation to the vesicle quantity per cell [5].
• A system for sialic acid transfer by colominic acid and a sialidase that preferentially hydrolyzes sialyl alpha-2,8 linkages [6].

Analytical, diagnostic and therapeutic context of BF3936

• After treatment, sialidase was detected in the vaginal fluid of 1 (5%) of 22 women who responded to therapy and in all of 6 women for whom therapy failed [2].
• The native sialidase had a molecular weight of 165kDa, as determined by Superose6 gel filtration chromatography and consisted of three subunits each of 55kDa by SDS-polyacrylamide gel electrophoresis [3].
• A commensal strain, previously defined as avirulent in an animal model, presented the lowest vesicle-associated sialidase activity and the greatest SV expression as opposed to what happened with clinical and environmental strains [5].

References