Ho C L, Lin Y L, Chen W C, Rocchi R, Piek T
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, R.O.C.
Toxicon. 1998 Jan;36(1):217-21. doi: 10.1016/s0041-0101(97)00066-4.
Three synthetic vespulakinin analogues either with or without carbohydrate moieties and mastoparan B isolated from Vespa basalis venom were investigated for their immunogenic activity and solution conformation. Mice immunized with these wasp venom peptides, with the exception of (Gal alpha)Thr3, (Gal alpha)Thr4-vespulakinin 1, showed positive antibody responses. However, the response elicited by mastoparan B was much higher than those induced by vespulakinin analogues. The class of antibody induced by these peptides was identified as an IgG1 isotype with kappa-light chain, suggesting stimulation of a T-cell-dependent immune response by these peptides. According to the circular dichroism spectra of these peptides, the structures of the vespulakinin analogues in solution were largely unordered, while mastoparan B exhibited a conformation rich in alpha-helices. The presence of carbohydrate moieties and the rather random structure in vespulakinins may interfere with T-cell recognition of the peptides, leading to lower immune responses.
研究了三种具有或不具有碳水化合物部分的合成黄蜂激肽类似物以及从黄蜂毒液中分离出的马斯托帕兰B的免疫原活性和溶液构象。用这些黄蜂毒液肽免疫的小鼠，除了（半乳糖α）苏氨酸3、（半乳糖α）苏氨酸4 - 黄蜂激肽1外，均表现出阳性抗体反应。然而，马斯托帕兰B引发的反应远高于黄蜂激肽类似物诱导的反应。这些肽诱导的抗体类别被鉴定为具有κ轻链的IgG1同种型，表明这些肽刺激了T细胞依赖性免疫反应。根据这些肽的圆二色光谱，溶液中黄蜂激肽类似物的结构大多无序，而马斯托帕兰B呈现出富含α螺旋的构象。黄蜂激肽中碳水化合物部分的存在以及相当随机的结构可能会干扰T细胞对这些肽的识别，导致较低的免疫反应。
