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Direct binding of herpes simplex virus type 1 virions to complement C3
Yen-Ting Chen1, Yi-Hui Wang, Yi-Yun Cheng
1Faculty of Dentistry, National Yang-Ming University, Pei-Tou, Taipei, Taiwan.
Viral Immunology
|October 30, 2003
Summary
Herpes simplex virus type 1 (HSV-1) virions directly bind human complement C3. This interaction is complement-dependent and heparin-inhibitable, with bound virions retaining infectivity.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Glycoprotein C (gC) of herpes simplex virus type 1 (HSV-1) is known to bind human complement C3.
- Previous studies indicated binding of purified gC or gC on infected cells to C3.
- Direct binding of intact HSV-1 virions to C3 was not clearly established.
Purpose of the Study:
- To investigate the direct binding interaction between purified HSV-1 virions and human complement C3.
- To determine if the binding is complement-dependent and if virion infectivity is maintained.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) to detect binding of purified HSV-1 virions (HSV-1(KOS) and HSV-1(hrR3)) to C3-coated plates.
- Assessment of virion infectivity by co-culturing captured virions with Vero cells.
- Heat inactivation of C3 and pre-incubation of virions with heparin to assess binding requirements.
Main Results:
- Direct binding of purified HSV-1 virions to C3-coated plates was demonstrated using ELISA.
- Captured virions on C3-coated plates remained infectious to Vero cells.
- Binding was abolished when C3 was heat-inactivated, indicating complement dependence.
- Heparin pre-incubation inhibited the interaction between virions and C3.
Conclusions:
- A direct interaction between HSV-1 virions and human complement C3 was confirmed.
- The binding interaction is dependent on active complement C3.
- Heparin can inhibit the binding of HSV-1 virions to C3.
- HSV-1 virions maintain their infectivity after binding to C3.