t Hart B A, Elferink D G, Drijfhout J W, Storm G, van Blooijs L, Bontrop R E, de Vries R R
Department of Immunobiology, Biomedical Primate Research Centre, Rijswijk, The Netherlands.
FEBS Lett. 1997 Jun 2;409(1):91-5. doi: 10.1016/s0014-5793(97)00493-6.
Amino acid residues 3-15 of mycobacterial HSP60 define a dominant T-cell epitope for HLA-DR3+ve humans and Mamu-DR3+ve rhesus monkeys. Our results show that Mamu-DR3 molecules on PBMC can be efficiently loaded in vivo with the above-mentioned peptides when they are intravenously injected encapsulated in liposomes, but not in the free form. Mamu-DR3 loading is abolished by encapsulation of a nonstimulatory peptide. These results have implications for the delivery of therapeutic peptides in vivo.
分枝杆菌热休克蛋白60（HSP60）的氨基酸残基3至15定义了HLA - DR3阳性人类和Mamu - DR3阳性恒河猴的主要T细胞表位。我们的结果表明，当包裹在脂质体中的上述肽静脉注射时，外周血单核细胞（PBMC）上的Mamu - DR3分子可以在体内有效地加载这些肽，但游离形式则不能。非刺激性肽的包裹会消除Mamu - DR3的加载。这些结果对体内治疗性肽的递送具有启示意义。
