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Related Experiment Videos

Herpes simplex virus glycoprotein C is a receptor for complement component iC3b.

R Tal-Singer1, C Seidel-Dugan, L Fries

  • 1Department of Medicine (School of Medicine), Children's Hospital of Philadelphia, PA.

The Journal of Infectious Diseases
|October 1, 1991
PubMed
Summary

Herpes simplex virus type 1 (HSV-1) infected cells bind complement C3 fragments, while HSV-2 infected cells do not. HSV-2 glycoprotein C (gC2) binds iC3b, suggesting a role similar to the complement receptor CR3.

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Area of Science:

  • Immunology
  • Virology
  • Molecular Biology

Background:

  • Herpes simplex viruses (HSV) are significant human pathogens.
  • Complement system activation plays a crucial role in antiviral immunity.
  • HSV glycoproteins, like glycoprotein C (gC), are involved in host-pathogen interactions.

Purpose of the Study:

  • To investigate the interaction of herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) infected cells with complement C3 fragments.
  • To determine the role of HSV-2 glycoprotein C (gC2) in binding complement fragments.
  • To map the domains on gC2 responsible for complement fragment binding.

Main Methods:

  • Cell surface binding assays using HSV-1 and HSV-2 infected cells.
  • Transfection assays with HSV-2 gC2 gene in mammalian cells.

Related Experiment Videos

  • Analysis of linker insertion mutants of gC2 to map binding domains.

    • Main Results:

    • HSV-1 infected cells bound C3b and iC3b, but not C3d.
    • HSV-2 infected cells did not bind any C3 fragments.
    • iC3b binding was mapped to gC2, specifically to three domains similar to C3b binding regions.
    • HSV-2 gC2 mediated iC3b binding to mammalian cells.

    Conclusions:

    • HSV-1 and HSV-2 exhibit differential binding to complement C3 fragments.
    • HSV-2 glycoprotein C (gC2) is responsible for binding iC3b.
    • The binding function of gC2 may be analogous to the mammalian complement receptor 3 (CR3).