鉴定由b型流感嗜血杆菌P1特异性单克隆抗体识别的表面暴露B细胞表位。
Identification of surface-exposed B-cell epitopes recognized by Haemophilus influenzae type b P1-specific monoclonal antibodies.
作者信息
Panezutti H, James O, Hansen E J, Choi Y, Harkness R E, Klein M H, Chong P
机构信息
Connaught Centre for Biotechnology Research, Willowdale, Ontario, Canada.
出版信息
Infect Immun. 1993 May;61(5):1867-72. doi: 10.1128/iai.61.5.1867-1872.1993.
Abstract
A panel of P1 synthetic peptides was synthesized to map the surface-exposed epitopes of Haemophilus influenzae type b outer membrane protein P1 recognized by three murine monoclonal antibodies (MAbs 7C8, 3E12, and 6B1). By using peptide-specific enzyme-linked immunosorbent assays, MAbs 6B1, 7C8, and 3E12 were shown to recognize distinct epitopes localized within residues 60 to 88, 165 to 193, and 400 to 437 of mature P1, respectively. Since MAb 7C8 was shown previously to be protective against certain H. influenzae type b subtypes in the infant rat model of bacteremia, its cognate epitope was further characterized by using truncated peptide analogs. Fine mapping of the 7C8 epitope by competitive inhibition studies revealed that it was localized within residues 184 and 193.
摘要
合成了一组P1合成肽，以绘制被三种鼠单克隆抗体（单克隆抗体7C8、3E12和6B1）识别的b型流感嗜血杆菌外膜蛋白P1的表面暴露表位。通过使用肽特异性酶联免疫吸附测定，显示单克隆抗体6B1、7C8和3E12分别识别位于成熟P1的60至88、165至193和400至437位残基内的不同表位。由于先前已证明单克隆抗体7C8在幼鼠菌血症模型中对某些b型流感嗜血杆菌亚型具有保护作用，因此通过使用截短的肽类似物对其同源表位进行了进一步表征。通过竞争性抑制研究对7C8表位进行精细定位，结果显示它位于184和193位残基内。
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