Robinson J H, Case M C, Brooks C G
Department of Immunology, The Medical School, University of Newcastle upon Tyne, U.K.
Immunology. 1992 Aug;76(4):593-8.
The effect on antigenicity of covalent attachment of lipid groups to a protein antigen was investigated. Coupling of palmitic acid to ovalbumin (OVA) enhanced major histocompatibility complex (MHC) class II-restricted presentation to most OVA-specific murine T-cell clones in vitro. The enhanced antigenicity of palmitoylated antigen was localized to the level of presentation of the synthetic peptide epitope, OVA 323-339. T-cell responses to palmitoylated antigen were more difficult to block with anti-MHC class II antibodies than responses to native antigen. However, T-cell proliferation to palmitoyl (p)-OVA and native (n)-OVA were blocked equally by anti-CD4 antibodies. Taken together, the results suggest that lipid conjugation of a protein antigen leads to the formation of a lipopeptide T-cell epitope with increased affinity of binding to MHC class II and/or T-cell receptor (TcR). These results have implications for the design of synthetic peptide vaccines.
研究了脂质基团与蛋白质抗原共价连接对抗抗原性的影响。将棕榈酸偶联到卵清蛋白（OVA）上，在体外增强了主要组织相容性复合体（MHC）II类限制的呈递，使其呈递给大多数OVA特异性小鼠T细胞克隆。棕榈酰化抗原增强的抗原性定位于合成肽表位OVA 323 - 339的呈递水平。与对天然抗原的反应相比，用抗MHC II类抗体更难阻断T细胞对棕榈酰化抗原的反应。然而，抗CD4抗体对棕榈酰（p）-OVA和天然（n）-OVA的T细胞增殖的阻断作用相同。综上所述，结果表明蛋白质抗原的脂质偶联导致形成一种脂肽T细胞表位，其与MHC II类和/或T细胞受体（TcR）的结合亲和力增加。这些结果对合成肽疫苗的设计具有启示意义。
