吸附于明矾的酿酒酵母重组Pfs25可引发能阻断恶性疟原虫传播的抗体。
Saccharomyces cerevisiae recombinant Pfs25 adsorbed to alum elicits antibodies that block transmission of Plasmodium falciparum.
作者信息
Kaslow D C, Bathurst I C, Lensen T, Ponnudurai T, Barr P J, Keister D B
机构信息
Molecular Vaccine Section, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892.
出版信息
Infect Immun. 1994 Dec;62(12):5576-80. doi: 10.1128/iai.62.12.5576-5580.1994.
Abstract
Antibodies to Pfs25, a cysteine-rich 25-kDa protein present on the surface of Plasmodium falciparum zygotes, can completely block the transmission of malaria parasites when mixed with infectious blood and fed to mosquitoes through a membrane feeding apparatus. Recently, a polypeptide analog, Pfs25-B, secreted from recombinant Saccharomyces cerevisiae was found to react with conformation-dependent, transmission-blocking monoclonal antibodies and to elicit transmission-blocking antibodies in experimental animals when emulsified in either Freund's or muramyl tripeptide adjuvant. In this study, Pfs25-B adsorbed to alum induced transmission-blocking antibodies in both rodents and primates. Bacterially produced Pfs25, however, did not elicit complete transmission-blocking antibodies in rodents. Furthermore, unlike monoclonal antibodies to Pfs25, which block transmission only after ookinete development, antisera to Pfs25-B adsorbed to alum appeared to block the in vivo development of zygotes to ookinetes as well.
摘要
Pfs25是一种存在于恶性疟原虫合子表面的富含半胱氨酸的25 kDa蛋白质，其抗体与感染性血液混合并通过膜饲器喂给蚊子时，可完全阻断疟原虫的传播。最近发现，重组酿酒酵母分泌的一种多肽类似物Pfs25-B可与构象依赖性、阻断传播的单克隆抗体发生反应，当在弗氏佐剂或胞壁酰三肽佐剂中乳化时，可在实验动物中引发阻断传播的抗体。在本研究中，吸附于明矾的Pfs25-B在啮齿动物和灵长类动物中均诱导出阻断传播的抗体。然而，细菌产生的Pfs25在啮齿动物中并未引发完全阻断传播的抗体。此外，与仅在动合子发育后才阻断传播的Pfs25单克隆抗体不同，吸附于明矾的Pfs25-B抗血清似乎也能阻断合子在体内发育为动合子。
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