Characterization of a human monoclonal antibody obtained after immunization with plasma vaccine and a booster with recombinant-DNA hepatitis B vaccine
Characterization of a human monoclonal antibody obtained after immunization with plasma vaccine and a booster with recombinant-DNA hepatitis B vaccine
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DOI：
10.1002/jmv.2146
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发表时间：
2002-03-01
影响因子：
12.7
通讯作者：
Osterhaus, ADME
中科院分区：
文献类型：
--
作者：
Heijtink, RA;Kruining, J;Osterhaus, ADME
人单克隆抗体类型 IgG4，命名为 1Ff4，是在酵母重组 DNA 衍生疫苗 (Engerix-B) 一次加强后，通过 Epstein Barr 病毒转化乙型肝炎疫苗接种者 (HB-VAX：血浆衍生疫苗) 的外周血淋巴细胞获得的。 1Ff4 优先结合 HBsAg/adw(2) 和 HBsAg/ayw(1)。在结合实验中，它与接种 HB-VAX-DNA（重组酵母）和 HB-VAX（血浆衍生疫苗）诱导的抗体竞争。 1Ff4 部分与单克隆抗体竞争 w/r 区域。检测到 HBsAg/adw(2) 与固相抗 HBs 结合的部分抑制，类似于使用“a”环特异性的其他人单克隆抗体获得的抑制。 1Ff4 不与覆盖两个“a”环的线性肽或 adw(2)/G145R 突变体结合，其与野生型 HBsAg 的结合强烈依赖于二硫键的存在。在来自流行区的大量 HBsAg 阳性样本中，1Ff4 抗体成功用于区分 adw(2) 和 adrq+ 菌株。 1Ff4 和其他人单克隆抗 HBs 抗体的表征可能有助于了解免疫引起的保护性抗体的精细特异性。 (C) 2002 Wiley-Liss, Inc.
A human monoclonal antibody type IgG4, designated 1Ff4 was obtained by Epstein Barr virus transformation of peripheral blood lymphocytes from a hepatitis B vaccinee (HB-VAX: plasma-derived vaccine) after one boost of yeast recombinant DNA derived vaccine (Engerix-B). 1Ff4 binds preferentially to HBsAg/adw(2) and HBsAg/ayw(1). In binding experiments, it competes with antibodies induced by vaccination with HB-VAX-DNA (yeast recombinant) and HB-VAX (plasma-derived vaccine). 1Ff4 competes in part with a monoclonal antibody for the w/r region. Partial inhibition of binding of HBsAg/adw(2) to solid phase anti-HBs was detected, resembling inhibition obtained using other human monoclonal specific for the "a"-loop. 1Ff4 does not bind to linear peptides covering the two "a"-loops or to an adw(2)/G145R mutant, its binding to wild type HBsAg strongly depends on the presence of disulphide bonds. In a large series of HBsAg-positive samples from an endemic area, 1Ff4 antibodies were successfully used to discriminate between an adw(2) and an adrq+ strain. The characterisation of 1Ff4 and other human monoclonal anti-HBs antibodies may help to understand the fine specificity of protective antibodies elicited by immunization. (C) 2002 Wiley-Liss, Inc.