Herpes simplex virus binds to human serum lipoprotein.

摘要: Binding of herpes simplex virus (HSV) type 1 to the various subclasses human serum lipoproteins was investigated. Studies were performed with purified by differential ultracentrifugation and artificial proteoliposomes containing only one apolipoprotein (A1, E) using an enzyme-linked immunosorbent assay technique, column chromatography, electron microscopy. All tested lipoprotein (very low, low-, high-density lipoproteins; VLDL, LDL, HDL, HDL1) showed significant binding HSV 1. Furthermore, bound all different synthetic proteoliposomes. Adsorption envelope proteins isolated from Sepharose-bound revealed glycoprotein B. Based on these results we reached conclusion that in HSV-lipoprotein complex formation lipid component B are preferential reaction partners.