PAROVIRUS (HUMAN) B19

我们的实验室对B19细小病毒进行基础和临床研究， 细小病毒科中在人类身上致病的唯一成员。急性 感染导致第五种疾病，一种儿童皮疹疾病和一种 成人多关节痛综合征。在患有潜在疾病的患者中 溶血、急性感染导致一过性再生障碍性危象。在……里面 有潜在免疫缺陷的患者，病毒感染持续存在 导致慢性贫血；细小病毒感染是导致贫血的原因之一 艾滋病患者。该病毒对红系祖细胞是嗜好的。 在过去的一年里，在三个方面取得了进展：1)病毒 结构；2)免疫原性和疫苗配方；3)非结构 蛋白质结构和功能。我们已经确定了细胞受体 对于B19细小病毒作为球蛋白或P抗原，存在于红色上的糖脂 细胞和红系前体细胞。B19的晶体结构 细小病毒空衣壳已在低分辨率下被确定，并显示 预期与犬细小病毒结构相似，以及 表面构象有显著差异。为了免疫原性 研究表明，微小衣壳蛋白的独特区域已被证明 含有能够激发中和抗体活性的有效线性表位 在动物身上。我们已经证明，VP1的浓缩大大增加了 三种动物的中和抗体反应；剂量范围 佐剂研究已经完成，为人类疫苗做准备 审判。最后，B19细小病毒的重组非结构蛋白 用高压液相色谱分离纯化。一颗核子 已确定本地化区域。

Our laboratory performs basic and clinical studies of the B19 parvovirus, the only member of the Parvoviridae family pathogenic in humans. Acute infection causes fifth disease, a childhood rash illness and a polyarthralgia syndrome in adults. In patients with underlying hemolysis, acute infection results in transient aplastic crisis. In patients with underlying immunodeficiency, virus infection persists and causes chronic anemia; parvovirus infection is a cause of anemia in patients with AIDS. The virus is tropic for erythroid progenitor cells. During the past year, progress has been made in three areas: 1) virus structure; 2)immunogenicity and vaccine formulation; 3)non-structural protein structure and function. We have identified the cellular receptor for B19 parvovirus as globoside or P antigen, a glycolipid present on red cells and erythroid precursor cells. The crystal structure of B19 parvovirus empty capsids has been determined at low resolution and shows expected similarities to the structure of canine parvovirus as well as a remarkable difference in the surface conformation. For immunogenicity studies, the unique region of the minor capsid protein has been shown to contain potent linear epitopes that elicit neutralizing antibody activity in animals. We have shown that enrichment for VP1 greatly increases the neutralizing antibody response in three species of animals; dose ranging and adjuvant studies have been completed in preparation for human vaccine trials. Finally, recombinant nonstructural protein of B19 parvovirus has been purified using high pressure liquid chromatography. A nuclear localizing region has been identified.