Direct binding of herpes simplex virus type 1 virions to complement C3.
Glycoprotein C (gC) of type 1 herpes simplex virus (HSV-1) binds the human complement C3 as purified proteins, or when expressed on the surface of infected cells. However, it is not clear whether the purified HSV virion binds directly to C3. In this study, direct binding of purified virions, HSV-1(KOS) or HSV-1(hrR3), to C3-coated plate was demonstrated by an enzyme-linked immunosorbent assay (ELISA). Captured virions on C3-coated plates were still infectious as determined by adding Vero cells to allow for infection to occur. The binding of virions to C3 was abolished if C3 was heat-inactivated, confirming a requirement for complement. In addition, the interaction was inhibited by preincubation of purified virions with heparin. In conclusion, a direct interaction of C3 with the HSV-1 virions was demonstrated.
Faculty of Dentistry, National Yang-Ming University, Pei-Tou, Taipei, Taiwan.
Yen-Ting
YT
Chen
Yi-Hui
YH
Wang
Yi-Yun
YY
Cheng
Shan-Ling
SL
Hung
D000818:Animals; D002522:Chlorocebus aethiops; D003167:Complement Activation; D003176:Complement C3 / Q000378:metabolism*; D003588:Cytopathogenic Effect, Viral / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D018259:Herpesvirus 1, Human / Q000276:immunology* / Q000472:pathogenicity; D006801:Humans; D066298:In Vitro Techniques; D011485:Protein Binding; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000276:immunology* / Q000378:metabolism
D003176:Complement C3; D014759:Viral Envelope Proteins; C038535:glycoprotein gC, herpes simplex virus type 1