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Purification and characterization of vims-like particles and pentamers produced by the expression of SV40 capsid proteins in insect cells

机译:SV40衣壳蛋白在昆虫细胞中表达产生的病毒样颗粒和五聚体的纯化和表征

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摘要

Three capsid proteins oi' SV40 (VP1, VP2, and VP3) were expressed in insect cells using recombinant baculoviruses. When the VP1 eupskl protein was expressed alone or co-expressed with VP2 and VP3, virus-like particles (VLP) were produced. In the latter case, the minor capsid proteins, VP2 and VP3, were incorporated into the VLP. VLPs with and without VP2 and VP3, and the wild type SV40 virions were indistinguishable under electron microscope. The sedimentation coefficient, v-,Uw, obtained for the VLP consisting of VP1 iilone (VPI-VI.P) was 170 S, and that for the VLP consisting of all of the capsid proteins (VPt/2/3-VLP) was 174 S. Treatment of the VI11 VLP with a calcium ion dictating agent and a reducing agent caused dissociation of the VP1 -VLP. The dissociated and purified VP1 pmieins were identified as pentamers of VP1 based on the molecular weight determination by sedimentation equilibrium. The pentamers were shown to possess the ability to re-assemble into VLP which had the s20w of 141S. The results are discussed in relation to the morphogenesis of SV40.
机译:使用重组杆状病毒在昆虫细胞中表达了三种衣壳蛋白oi'SV40(VP1,VP2和VP3)。当VP1 eupskl蛋白单独表达或与VP2和VP3共表达时,会产生病毒样颗粒(VLP)。在后一种情况下,次要衣壳蛋白VP2和VP3被并入VLP。在电子显微镜下,带有和不带有VP2和VP3的VLP以及野生型SV40病毒体是无法区分的。由VP1 iilone(VPI-VI.P)组成的VLP的沉降系数v-,Uw为170 S,由所有衣壳蛋白(VPt / 2 / 3-VLP)组成的VLP的沉降系数为v。 174S。用钙离子指示剂和还原剂处理VI11 VLP引起VP1-VLP的解离。根据通过沉降平衡测定的分子量,将解离和纯化的VP1 pmieins鉴定为VP1的五聚体。证明五聚体具有重新组装成SLP为141S的VLP的能力。讨论了有关SV40形态的结果。

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