Crystal Structure of the HSV-1 Fc Receptor Bound to Fc Reveals a Mechanism for Antibody Bipolar Bridging
2006
How Herpes Evades the Immune System
publication
Evidence: moderate
Author Information
Author(s): Elizabeth Sprague, Pamela Bjorkman
Hypothesis
How does the herpes simplex virus type-1 (HSV-1) evade the immune response mediated by antibodies?
Conclusion
The study reveals that HSV-1 uses a protein complex to incapacitate antibodies, aiding its survival in the host.
Supporting Evidence
- The study identified how the gE-gI complex binds to antibodies, preventing their function.
- Structural analysis revealed the pH-dependent nature of the gE-gI/Fc interaction.
- The findings suggest a mechanism for HSV-1 to evade immune detection by utilizing bipolar bridging.
Takeaway
Herpes has a clever way of avoiding the body's defenses by using a special protein to grab onto antibodies and stop them from working.
Methodology
The researchers used assays to measure binding and X-ray crystallography to determine the structure of the gE-gI/Fc complex.
Digital Object Identifier (DOI)
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