UNIQUE REGION OF THE MINOR CAPSID PROTEIN OF HUMAN PARVOVIRUS B19 IS EXPOSED ON THE VIRION SURFACE
UNIQUE REGION OF THE MINOR CAPSID PROTEIN OF HUMAN PARVOVIRUS B19 IS EXPOSED ON THE VIRION SURFACE
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DOI：
10.1172/jci115812
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发表时间：
1992-06-01
影响因子：
15.9
通讯作者：
COLLETT, MS
中科院分区：
文献类型：
--
作者：
ROSENFELD, SJ;YOSHIMOTO, K;COLLETT, MS
B19 细小病毒的衣壳由主要（VP2；58 kD）和次要（VP1；83 kD）结构蛋白组成。除了 VP1 氨基末端有一个独特的 226 个氨基酸区域外，这些蛋白质是相同的。先前的重组空衣壳免疫研究已证明，需要 VP1 的存在才能引发病毒中和抗体活性。然而，迄今为止，仅在 VP2 上鉴定出中和表位。对相关细小病毒（犬细小病毒）的晶体学研究表明，VP1 独特的氨基末端部分位于病毒衣壳内的内部位置。为了确定 VP1 在空衣壳和病毒粒子中的位置，我们表达了包含 VP1 独特区域的融合蛋白。在酶联免疫吸附测定中，针对该蛋白产生的抗血清可识别含有 VP1 和 VP2 的重组空衣壳，但不能识别仅含有 VP2 的重组空衣壳。抗血清免疫沉淀重组空衣壳和人血浆衍生的病毒粒子，并如免疫电子显微镜所示凝集后者。该血清含有有效的体外病毒感染性中和活性。这些数据表明VPI的氨基末端的一部分位于病毒体表面，并且该区域包含内在的中和决定簇。 VP1 特异性尾部的外部位置可能为新型重组疫苗中的工程异源表位呈现提供位点。
Capsids of the B19 parvovirus are composed of major (VP2; 58 kD) and minor (VP1; 83 kD) structural proteins. These proteins are identical except for a unique 226 amino acid region at the amino terminus of VP1. Previous immunization studies with recombinant empty capsids have demonstrated that the presence of VP1 was required to elicit virus-neutralizing antibody activity. However, to date, neutralizing epitopes have been identified only on VP2. Crystallographic studies of a related parvovirus (canine parvovirus) suggested the unique amino-terminal portion of VP1 assumed an internal position within the viral capsid. To determine the position of VP1 in both empty capsids and virions, we expressed a fusion protein containing the unique region of VP1. Antisera raised to this protein recognized recombinant empty capsids containing VP1 and VP2, but not those containing VP2 alone, in an enzyme-linked immunosorbent assay. The antisera immunoprecipitated both recombinant empty capsids and human plasma-derived virions, and agglutinated the latter as shown by immune electron microscopy. The sera contained potent neutralizing activity for virus infectivity in vitro. These data indicate that a portion of the amino terminus of VPI is located on the virion surface, and that this region contains intrinsic neutralizing determinants. The external location of the VP1-specific tail may provide a site for engineered heterologous epitope presentation in novel recombinant vaccines.