Williams K M, Sacci J B, Anthony R L
J Immunol. 1986 Mar 1;136(5):1853-8.
A murine monoclonal antibody (83L-2D3/a) to a dominant surface antigen of Leishmania braziliensis panamensis (WRAIR-470) recognized a determinant expressed on the surface membrane of mouse peritoneal macrophages infected in vitro. This determinant, also demonstrable on the surface membrane of intracellular amastigotes, was not displayed by the macrophage until at least 6 hr post-infection. This delay in expression and the obvious negativity of all uninfected macrophages inherent to infected cultures implied that the leishmania determinant had an intracellular origin. Furthermore, expression was dependent upon maintenance of macrophage function. When the parasite burden became overwhelming, additional antigen processing ceased, and that which had accumulated was either shed into the medium or was internalized. Immunochemical analyses revealed that the 83L-2D3/a reactive epitope was part of a 15,000 dalton molecule, which in all likelihood represents a breakdown product of a major surface glycoconjugate that had been degraded in the phagolysosome.
一种针对巴拿马利什曼原虫(WRAIR - 470)主要表面抗原的鼠单克隆抗体(83L - 2D3/a)识别出一种在体外感染的小鼠腹膜巨噬细胞表面膜上表达的决定簇。这种决定簇在细胞内无鞭毛体的表面膜上也可显示,但巨噬细胞直到感染后至少6小时才显示该决定簇。这种表达延迟以及感染培养物中所有未感染巨噬细胞固有的明显阴性表明利什曼原虫决定簇起源于细胞内。此外,表达依赖于巨噬细胞功能的维持。当寄生虫负荷变得过重时,额外的抗原加工停止,积累的抗原要么释放到培养基中,要么被内化。免疫化学分析表明,83L - 2D3/a反应性表位是一个15,000道尔顿分子的一部分,极有可能代表在吞噬溶酶体中降解的主要表面糖缀合物的分解产物。