Son, Eui-Sun
(Department of Parasitology and Catholic Institute of Parasitic Diseases, Catholic University of Korea, College of Medicine)
,
Nam, Ho-Woo
(Department of Parasitology and Catholic Institute of Parasitic Diseases, Catholic University of Korea, College of Medicine)
Excretory/secretory proteins (ESP) from Toxoplasma gondii were analyzed to define the function in the penetration process into host cells. Whole ESP obtained at 37$^{\circ}C$ were composed of 15 bands with molecular mass of 110, 97, 86, 80, 70, 60, 54, 42, 40, 36. 30, 28, 26, 22, and 19 k...
Excretory/secretory proteins (ESP) from Toxoplasma gondii were analyzed to define the function in the penetration process into host cells. Whole ESP obtained at 37$^{\circ}C$ were composed of 15 bands with molecular mass of 110, 97, 86, 80, 70, 60, 54, 42, 40, 36. 30, 28, 26, 22, and 19 kDa. Five ESP of 86, 80, 42, 36, and 28 kDa were reacted with monoclonal antibodies (mAb). named as Tg386 (microheme), Tg485 (surface membrane), Tg786 (rhoptry), Tg378, and Tg556 (both dense granules), respectively. The ESP was released by a temperature-dependent/-independent manner and all at once whenever ready to pour out except Tg786. Each ESP was not exhausted within the parasite but the amount was limited. Tg786 was released continuously with increment, whereas Tg378 and Tg556 were ceased to release after 3 and 4 hr, Dense granular Tg378 and Tg556 were released spontaneously and constitutively before the entry into host cells also. The entry of T. gondii was inhibited by all the mAbs differentially. And the parasite deprived of ESP was inhibited to enter exponentially up to 90.1%. It is suggested that ESP play an essential function to provide appropriate environment for the entry of the parasite into host cells.
Excretory/secretory proteins (ESP) from Toxoplasma gondii were analyzed to define the function in the penetration process into host cells. Whole ESP obtained at 37$^{\circ}C$ were composed of 15 bands with molecular mass of 110, 97, 86, 80, 70, 60, 54, 42, 40, 36. 30, 28, 26, 22, and 19 kDa. Five ESP of 86, 80, 42, 36, and 28 kDa were reacted with monoclonal antibodies (mAb). named as Tg386 (microheme), Tg485 (surface membrane), Tg786 (rhoptry), Tg378, and Tg556 (both dense granules), respectively. The ESP was released by a temperature-dependent/-independent manner and all at once whenever ready to pour out except Tg786. Each ESP was not exhausted within the parasite but the amount was limited. Tg786 was released continuously with increment, whereas Tg378 and Tg556 were ceased to release after 3 and 4 hr, Dense granular Tg378 and Tg556 were released spontaneously and constitutively before the entry into host cells also. The entry of T. gondii was inhibited by all the mAbs differentially. And the parasite deprived of ESP was inhibited to enter exponentially up to 90.1%. It is suggested that ESP play an essential function to provide appropriate environment for the entry of the parasite into host cells.
* AI 자동 식별 결과로 적합하지 않은 문장이 있을 수 있으니, 이용에 유의하시기 바랍니다.
제안 방법
And then dense granular proteins are secreted into the PV and PVM continuously during the intracellular residence of the parasite (Leriche and Dubremetz, 1990; Cesbron-Delauw, 1994). In this work, we attempted to profile the production, subcellular localization, and exhaustion of excretory/secretory proteins (ESP). And also, we pursued the possible role of the ESP on the penetrating activity of T.
성능/효과
, 2000). Among the 5 proteins of 86, 80, 42, 36, and 28 kDa detected by mAbsof Tg386, Tg485, Tg786, Tg378, and Tg556 clones, only Tg786 were released much longer with rapid increment in amount. It suggests that the ESP are released all at once whenever ready to pour out except that of Tg786 clone.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.