VAR2CSA domains expressed in Escherichia coli induce cross-reactive antibodies to native protein
VAR2CSA domains expressed in Escherichia coli induce cross-reactive antibodies to native protein
复制标题
DOI：
10.1086/529526
复制
发表时间：
2008-04-15
影响因子：
6.4
通讯作者：
Duffy, Patrick E.
中科院分区：
文献类型：
--
作者：
Oleinikov, Andrew V.;Francis, Susan E.;Duffy, Patrick E.
变异表面抗原VAR 2CSA是妊娠疟疾疫苗候选者，但其大小和多态性是开发的障碍。我们在大肠杆菌中表达了3D 7型VAR 2CSA结构域，作为变性和重折叠的不溶性His标记蛋白（Duffy结合样[DBL]结构域DBL 1，DBL 3，DBL 4和DBL 5）或作为可溶性谷胱甘肽S-转移酶标记蛋白（DBL 6）。抗DBL 5抗血清与硫酸软骨素A（CSA）结合实验室菌株（3D 7-CSA和FCR 3-CSA）和临床妊娠疟疾分离株的表面蛋白发生交叉反应，而抗DBL 6抗血清仅与3D 7表面蛋白发生反应。这是E.大肠杆菌表达的VAR 2CSA结构域诱导天然VAR 2CSA抗体。
The variant surface antigen VAR2CSA is a pregnancy malaria vaccine candidate, but its size and polymorphism are obstacles to development. We expressed 3D7-type VAR2CSA domains in Escherichia coli as insoluble His-tagged proteins (Duffy binding-like [DBL] domains DBL1, DBL3, DBL4, and DBL5) that were denatured and refolded or as soluble glutathione S-transferase -tagged protein (DBL6). Anti-DBL5 antiserum cross-reacted with surface proteins of chondroitin sulfate A (CSA)-binding laboratory strains (3D7-CSA and FCR3-CSA) and a clinical pregnancy malaria isolate, whereas anti-DBL6 antiserum reacted only to 3D7 surface protein. This is the first report that E. coli-expressed VAR2CSA domains induce antibody to native VAR2CSA.