Conraths F J, Hirzmann J, Hobom G, Zahner H
Institut für Parasitologie, Justus-Liebig-Universitat Giessen, Germany.
Exp Parasitol. 1997 Mar;85(3):241-8. doi: 10.1006/expr.1996.4138.
The microfilarial sheaths of the filarial parasites Brugia malayi, Brugia pahangi, and Litomosoides sigmodontis consist of several parasite proteins, probably ranging between 7 and 10. The gene encoding sheath protein 2 (shp2), which is the object of this study, is transcribed in embryos and in the uterine epithelium; at least in B. malayi, it is translated in both tissues. Apparently, shp2 is synthesized as a monomer, exported by the respective cells, and integrated into the microfilarial sheath. In the sheath, it exists as a highly polymerized molecule cross-linked by cysteine formation and other covalent bonds, presumably epsilon-(gamma-glutamyl)-lysine links.
马来布鲁线虫、彭亨布鲁线虫和sigmodontis丝虫的微丝蚴鞘由几种寄生虫蛋白组成,可能在7到10种之间。本研究的对象鞘蛋白2(shp2)的编码基因在胚胎和子宫上皮细胞中转录;至少在马来布鲁线虫中,它在这两种组织中都有翻译。显然,shp2以单体形式合成,由相应细胞输出,并整合到微丝蚴鞘中。在鞘中,它以高度聚合的分子形式存在,通过半胱氨酸形成和其他共价键交联,可能是ε-(γ-谷氨酰)-赖氨酸连接。