This monoclonal antibody which binds to the FbsA protein of Streptococcus agalactia may be useful in the treatment and protection against infections from S. agalactiae.
Figure 1 Inhibition of Fng binding to 6pGST by the 5H2mAb.
Goat anti-GST was immobilized on the wells of microtiterplates, followed by incubation with 6pGST (100 nM). Fng (500nM) was mixed with 1 µg/ml of mAb 5H2, mAb 10H1 or mouseIgG1 (isotype control) before being added to the wells. Afterwashing, Fng binding was detected using rabbit anti-Fngantibodies followed by alkaline phosphatase-conjugated goatanti-rabbit IgG.
Immunogenic Properties of Streptococcus agalactiae FbsA Fragments
Figure 2 Inhibition of GBS attachment to surface-coatedFng by the 5H2 mAb.
Cells of S. agalactiae 6313 (5x107) werepreincubated with the indicated amounts of mAbs 5H2 or 10H1,transferred to Fng-coated wells (1 µg/well) and the mixtureswere incubated for 2 hours. After extensive washes, 1 µg rabbitanti-GBS IgG was added to the wells, followed by a 90 minincubation. Adherent bacteria were detected by peroxidase-conjugated goat anti-rabbit IgG and the plates were developedwith o-phenylenediamine. All the data are expressed aspercentages of control adherence, where bacteria attachmentin the absence of antibody was set to 100% (equivalent to 0%inhibition). The bars show standard deviations of triplicatesamples. This experiment was performed three times withsimilar results.
Immunogenic Properties of Streptococcus agalactiae FbsA Fragments
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
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