SSL10 Antibody
Description
Binding Regions and Mechanisms
SSL10 interacts with multiple host proteins via distinct domains:
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N-terminal OB-fold domain: Binds human IgG1 (γ1 subclass) and inhibits complement C1q binding .
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C-terminal β-grasp domain: Binds fibrinogen, fibronectin, and coagulation factors (e.g., prothrombin) .
Chimera studies revealed SSL10’s IgG-binding activity is mediated by two regions:
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β1–β3 (N-terminal OB-fold): Critical for IgG1 recognition.
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β10–β12 (C-terminal β-grasp): Synergizes with β1–β3 for binding .
| Domain | Binding Partners | Functional Impact |
|---|---|---|
| N-terminal OB-fold | IgG1 Fc, ERK2 | Blocks FcγR binding, complement activation |
| C-terminal β-grasp | Fibrinogen, prothrombin | Disrupts coagulation, immune cell adhesion |
Functional Inhibition by SSL10 Antibodies
SSL10 Antibodies were tested for their ability to counteract SSL10’s immune-modulating effects:
IgG1-Mediated Phagocytosis
SSL10 binds IgG1 at residues Lys274/Asp276, Leu234/Leu235, and Lys322, which are critical for FcγR and C1q interactions . SSL10 Antibodies restored phagocytosis of IgG1-opsonized bacteria by blocking these interactions .
Complement Activation
SSL10 inhibits classical complement pathway activation by preventing C1q binding to IgG. SSL10 Antibodies reversed this inhibition, restoring C1q-mediated hemolysis .
Blood Coagulation
SSL10 binds prothrombin and factor Xa via γ-carboxyglutamic acid domains, impairing clotting. SSL10 Antibodies may restore coagulation by blocking these interactions .
Advantages
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Target specificity: SSL10 Antibodies show strict IgG1 and primate specificity, reducing off-target effects .
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Dual-domain inhibition: Simultaneous targeting of SSL10’s N- and C-terminal regions could enhance efficacy .
Challenges
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Cross-reactivity: SSL10 shares structural homology with other SSLs (e.g., SSL1, SSL5), necessitating careful epitope selection to avoid off-target binding .
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Delivery: ScFvs require optimization for half-life and tissue penetration in vivo .
Research Gaps and Future Directions
Product Specs
**Constituents:** 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
Q&A
Here’s a structured collection of FAQs for researchers studying SSL10 antibodies, optimized for academic rigor and methodological depth:
Advanced Research Questions
How does SSL10 structurally evade host immunity while targeting IgG1?
Mechanistic insights:
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SSL10’s N-terminal OB-fold domain binds the Cγ2 domain of IgG1 near Lys322 and Leu234/235, overlapping FcγR and C1q binding sites .
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Critical mutations:
What strategies overcome SSL10-induced phagocytosis blockade?
Therapeutic approaches:
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Engineered scFv antibodies: Phage-display libraries yield scFvs (e.g., clone #AH7) that restore neutrophil phagocytosis by 67% at 100 nM .
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Dual-target inhibitors: Small molecules disrupting both SSL10-IgG1 and SSL10-CXCR4 interactions (IC₅₀ = 12 μM) .
How do SSL10 variants across S. aureus strains impact virulence?
Data Contradiction Analysis
Discrepancies in reported SSL10 binding specificities
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Conflict: Early studies suggested pan-IgG binding , while recent work shows γ-1 specificity .
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Resolution:
Challenges in SSL10 antibody development
Technical Optimization
Improving SSL10 detection sensitivity in complex samples
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Immunoprecipitation-MS: Anti-SSL10 nanobodies coupled to magnetic beads (LOD = 0.1 ng/mL) .
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Multiplex assays: Combine Luminex xMAP® technology with SSL10-specific aptamers .
10. Validating SSL10’s role in necroptosis pathways
Stepwise protocol:
