Muster T, Guinea R, Trkola A, Purtscher M, Klima A, Steindl F, Palese P, Katinger H
Institut für Angewandte Mikrobiologie, Universität für Bodenkultur, Vienna, Austria.
J Virol. 1994 Jun;68(6):4031-4. doi: 10.1128/JVI.68.6.4031-4034.1994.
Previously we identified the highly conserved amino acids Glu-Leu-Asp-Lys-Trp-Ala (ELDKWA) on the ecto-domain of gp41 as the epitope of a neutralizing monoclonal antibody (2F5) directed against human immunodeficiency virus type 1. In the present study, the sequence defining the epitope was introduced into the loop of antigenic site B of the influenza virus hemagglutinin. The resulting chimeric virus was able to elicit ELDKWA-specific immunoglobulins G and A in antisera of mice. Moreover, the distantly related human immunodeficiency virus type 1 isolates MN, RF, and IIIB were neutralized by these antisera. These data suggest that this conserved B-cell epitope is a promising candidate for inclusion in a vaccine against AIDS. The results also show that influenza virus can be used to effectively present the antigenic structure of this B-cell epitope.
此前,我们将gp41胞外结构域上高度保守的氨基酸序列Glu-Leu-Asp-Lys-Trp-Ala(ELDKWA)鉴定为一种针对1型人类免疫缺陷病毒的中和单克隆抗体(2F5)的表位。在本研究中,将确定该表位的序列引入流感病毒血凝素抗原位点B的环中。所得嵌合病毒能够在小鼠抗血清中引发针对ELDKWA的免疫球蛋白G和A。此外,这些抗血清可中和亲缘关系较远的1型人类免疫缺陷病毒分离株MN、RF和IIIB。这些数据表明,这个保守的B细胞表位有望成为艾滋病疫苗的组成部分。结果还表明,流感病毒可用于有效呈递该B细胞表位的抗原结构。