ABSTRACT
To explore the role of lipid raft in assembly of human herpesvirus 6, the HHV-6 GS strain was applied to infect the HSB2 cells and then the lipid raft composition was extracted from the cells with non-ionic detergent Triton-X 100. The relationship between the HHV-6 envelope glycoprotein and lipid raft was analyzed by Western Blot. Immunofluorescence double-staining was used to study the colocalization of the HHV-6 glycoprotein B(gB) with GPI anchored protein CD59 and ganglioside GM respectively. HHV-6 envelope glycoprotein B, H, L, Q1 and Q2 (gB, gH, gL, gQ1 and gQ2) were all existed in the lipid raft. Moreover, CD59 and HHV-6 envelope glycoprotein B showed the same localization through the confocal microscope. We concluded the lipid raft provided the platform for HHV-6 assembly. This is the first report concerning to the role of lipid raft in assembly of human Herpesvirus 6.