Brandriss M W, Schlesinger J J, Walsh E E
Rochester General Hospital, New York.
J Infect Dis. 1990 Jun;161(6):1134-9. doi: 10.1093/infdis/161.6.1134.
Information on the immunogenic properties of purified flavivirus proteins may be useful in the development of recombinant or synthetic peptide vaccines. Using a monoclonal antibody, an attempt was made to purify the envelope (E) protein of 17D yellow fever virus (17D YF) by affinity chromatography. The purified material could not be identified as intact E protein but it did bear antigenic determinants of E as determined by selective reactivity with anti-E monoclonal antibodies. Rabbits immunized with this material produced antibodies that neutralized 17D YF and dengue-2 viruses in comparable titers, indicating that cross-reactive antigenic determinants were preserved. Immunization of mice resulted in protection against intracerebral challenge with 17D YF.
纯化黄病毒蛋白的免疫原性特性信息可能有助于重组或合成肽疫苗的研发。利用单克隆抗体,尝试通过亲和层析法纯化17D黄热病毒(17D YF)的包膜(E)蛋白。纯化后的物质无法鉴定为完整的E蛋白,但通过与抗E单克隆抗体的选择性反应确定其确实带有E蛋白的抗原决定簇。用该物质免疫的兔子产生了能以相当效价中和17D YF和登革2型病毒的抗体,表明交叉反应性抗原决定簇得以保留。用其免疫小鼠可使其免受17D YF脑内攻击。