Bourgeois C, Corvaisier C, Bour J B, Kohli E, Pothier P
Laboratory of Virology, Faculty de Médecine Dijon, France.
J Gen Virol. 1991 May;72 ( Pt 5):1051-8. doi: 10.1099/0022-1317-72-5-1051.
Chemical and enzymic cleavages of the F1 subunit of the fusion (F) protein of respiratory syncytial (RS) virus showed that the sequence 184-Gly to 314-Trp reacted with neutralizing monoclonal antibodies (MAbs). Twelve synthetic peptides covering a part of this sequence were analysed for their immunoreactivity with neutralizing MAbs and anti-RS virus rabbit serum. Two sequential antigenic domains corresponding to amino acids 200 to 225 and 255 to 278 were defined with anti-RS virus rabbit serum. The peptides 205-225 and 259-278, belonging to these antigenic domains, inhibited binding to the F protein and the neutralizing activity of the anti-RS virus rabbit serum. One MAb (RS-348) reacted with peptides containing amino acids 200 to 225. Moreover, the peptide 205-225 induced an anti-peptide rabbit serum neutralizing RS virus in vitro. These results indicate that the sequence from residues 200 to 225 was present in one of the immunodominant sites of the F protein.
呼吸道合胞（RS）病毒融合（F）蛋白F1亚基的化学和酶切分析表明，184位甘氨酸至314位色氨酸的序列与中和单克隆抗体（MAb）发生反应。分析了覆盖该序列一部分的12条合成肽与中和MAb和抗RS病毒兔血清的免疫反应性。用抗RS病毒兔血清确定了与氨基酸200至225和255至278相对应的两个连续抗原结构域。属于这些抗原结构域的肽205 - 225和259 - 278抑制了与F蛋白的结合以及抗RS病毒兔血清的中和活性。一种MAb（RS - 348）与含有氨基酸200至225的肽发生反应。此外，肽205 - 225诱导产生的抗肽兔血清在体外可中和RS病毒。这些结果表明，200至225位残基的序列存在于F蛋白的一个免疫显性位点中。
