Söderlund M, Brown C S, Cohen B J, Hedman K
Department of Virology, University of Helsinki, Finland.
J Infect Dis. 1995 Mar;171(3):710-3. doi: 10.1093/infdis/171.3.710.
In an attempt to improve diagnosis of illnesses caused by parvovirus B19 and to discriminate primary from secondary infections, a protein-denaturing assay for avidity of parvovirus-specific IgG antibodies was developed. The assay used three types of purified recombinant antigens: a fusion protein containing the unique portion of the structural protein VP1, entire capsids made up of the major structural protein VP2 alone, or VP2 plus VP1. The avidity assays were evaluated by testing sequential acute-phase serum samples from 61 well-characterized patients (34 were followed > or = 6 months), sera from 38 controls with evidence of past infection, and sera from 388 seropositive patients studied for evidence of B19 infection during an epidemic. Parvovirus capsids consisting of VP2 alone yielded unusual IgG avidity and IgG antibody responses. Three different IgG avidity assays based on VP1 protein antigens were highly sensitive and specific and were considered suitable for identification of recent primary infections by human parvovirus B19.
为了改善对细小病毒B19引起疾病的诊断,并区分原发性感染和继发性感染,开发了一种检测细小病毒特异性IgG抗体亲和力的蛋白质变性检测方法。该检测使用了三种类型的纯化重组抗原:一种含有结构蛋白VP1独特部分的融合蛋白、仅由主要结构蛋白VP2组成的完整衣壳,或VP2加VP1。通过检测61例特征明确的患者(34例随访≥6个月)的连续急性期血清样本、38例有既往感染证据的对照血清,以及388例在一次流行期间研究细小病毒B19感染证据的血清阳性患者的血清,对亲和力检测进行了评估。仅由VP2组成的细小病毒衣壳产生了异常的IgG亲和力和IgG抗体反应。基于VP1蛋白抗原的三种不同IgG亲和力检测方法具有高度敏感性和特异性,被认为适用于鉴定人细小病毒B19近期原发性感染。