Gardnerella vaginalis Vaginolysin Specific Neutra™ Antibody Products
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Are you currently facing long drug development cycles, difficulty in high-specificity target validation, or challenges in developing effective non-antibiotic therapeutics for bacterial infections? Our G. vaginalis Vaginolysin Specific Neutra™ Antibody Products help you accelerate drug discovery and obtain high-quality, biologically active reagents through innovative neutralizing antibody engineering techniques.
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Introduction of G. vaginalis Vaginolysin
Gardnerella vaginalis is a predominant bacterium strongly implicated in bacterial vaginosis (BV), a prevalent state of vaginal dysbiosis. BV is characterized by a shift away from beneficial Lactobacillus flora, resulting in adverse health consequences, including increased risk of preterm birth and STIs.
Vaginolysin (VLY) is the primary virulence factor of G. vaginalis. It is a potent pore-forming toxin (PFT), belonging to the Cholesterol-Dependent Cytolysin (CDC) family.
- Structure and Function: VLY is a ~57 kDa protein that forms lytic pores in host cell membranes by binding to cholesterol and oligomerizing. Critically, VLY exhibits human specificity because its pore-forming activity is strongly enhanced by binding to the human complement regulatory molecule CD59.
- Mechanism in Disease: At lytic concentrations, VLY causes direct lysis of vaginal epithelial cells. At lower (sublytic) concentrations, it initiates complex signaling cascades, such as activating the p38 MAPK pathway and inducing interleukin-8 (IL-8). This cellular disruption and inflammatory response drive epithelial damage and breach the mucosal barrier, establishing VLY as a primary driver of tissue pathology in BV.
Fig.1 A schematic illustration of current standard antibiotics developing resistance in BV.1
Antibodies Against G. vaginalis Vaginolysin
Targeting bacterial PFTs with neutralizing antibodies is a proven strategy for therapeutic intervention, independent of antimicrobial resistance pathways. Creative Biolabs' VLY-specific antibodies tightly bind VLY, inhibiting its crucial steps of cell interaction and pore formation.
The applications of high-quality anti-Vaginolysin antibodies span the entire translational research pipeline:
- Neutralization Assays: The primary application is measuring the antibody's ability to inhibit VLY-mediated cell lysis (hemolysis or cytotoxicity). MAbs like the well-studied clone 9B4 (targeting a critical VLY epitope) have demonstrated strong neutralizing activity, blocking the toxin-target interaction.
- Detection and Quantification: Anti-VLY antibodies are essential for robust Western Blot analysis and developing sensitive Sandwich ELISAs for quantifying VLY in culture supernatants or clinical samples, which is vital for monitoring G. vaginalis virulence.
- Visualization and Research: These tools are used in Immunofluorescence (IF) to visualize VLY expression and association with host cells or biofilms, providing cellular-level insights into pathogenesis.
- Novel Therapeutic Design: Neutralizing antibodies, including recombinant Single-Chain Variable Fragment (scFv) formats, are being explored as potential agents for passive protection against VLY-induced damage, offering a path toward non-antibiotic BV treatments.
Why Choose Us?
We focus on virulence factors to provide reagents optimized for superior reliability in biological and therapeutic applications:
- Guaranteed Functional Neutralization: All Neutra™ antibodies are validated in physiologically relevant cell models to ensure they block VLY-mediated cytotoxicity.
- Exceptional Specificity & Consistency: Rigorous screening ensures minimal cross-reactivity with other CDCs. We use recombinant production for high-purity, defined formats, ensuring batch-to-batch consistency.
- Diverse Formats & Support: We offer full-length IgG and recombinant fragments (scFvs). Our expert team provides dedicated technical support for VLY assay development.
FAQs
Q: What is the primary functional difference between this antibody and standard detection antibodies?
A: These high-affinity antibodies block the toxin's biological activity—inhibiting pore formation and cell lysis—making them indispensable for therapeutic interventions and disease mechanism studies, unlike detection antibodies that merely visualize or quantify.
Q: In what specific assay models have these anti-toxin antibodies proven most effective?
A: They demonstrate high efficacy in in vitro functional assays, particularly human erythrocyte hemolysis and cytotoxicity assays using epithelial cell lines. Their strong neutralizing activity validates their therapeutic potential by disrupting the toxin-receptor interaction.
Q: Is there any concern about potential cross-reactivity?
A: Rigorous validation ensures the antibody recognizes unique VLY epitopes (like those crucial for CD59 interaction) while minimizing cross-reactivity with other CDCs, providing reliable, clean data.
Q: Can these antibodies be used to study Vaginolysin in the context of the G. vaginalis biofilm?
A: Yes, they are excellent for studying VLY within complex matrices, including immunofluorescence localization within biofilm structure or assessing neutralizing effects on biofilm-associated toxicity.
Q: Beyond functional blocking, what other research value do these reagents offer over purified recombinant toxin?
A: A high-affinity antibody acts as a critical modulator: it allows probing specific toxin domains, measuring toxin presence in clinical fluids, and serving as a gold standard control for functional assays. Recombinant formats also facilitate in vivo and non-traditional delivery studies.
Our G. vaginalis Vaginolysin Specific Neutra™ Antibody Products deliver the specificity and functional validation necessary to accelerate your diagnostic or therapeutic research programs. Leverage our two decades of expertise.
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REFERENCE
- Dalabehera, Manoj et al. "Natural Molecules, Nutraceuticals, and Engineered Nanosystems: A Comprehensive Strategy for Combating Gardnerella vaginalis-Induced Bacterial Vaginosis." Microorganisms vol. 13,10 2411. 21 Oct. 2025, Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/microorganisms13102411
