A poliovirus type 1 neutralization epitope is located within amino acid residues 93 to 104 of viral capsid polypeptide VP1.
A poliovirus type 1 neutralization epitope is located within amino acid residues 93 to 104 of viral capsid polypeptide VP1.
复制标题
1型脊髓灰质炎病毒中和表位位于病毒衣壳多肽VP1的氨基酸残基93至104内。
作者：
C. Wychowski;S. Werf;O. Siffert;R. Crainic;P. Bruneau;M. Girard
使用核酸酶Bal 31，在质粒pCW 119内编码衣壳多肽VP 1的脊髓灰质炎病毒1型cDNA序列内产生缺失。缺失质粒在大肠杆菌中表达的融合蛋白与针对脊髓灰质炎病毒衣壳多肽VP 1的兔免疫血清（α VP 1抗体）反应。它们还与脊髓灰质炎病毒1型中和单克隆抗体C3反应，但当缺失延伸至VP 1氨基酸90 - 104时失去反应性。蛋白质的计算机分析显示，在VP 1氨基酸93 - 103区域中亲水性氨基酸残基的局部密度较高。化学合成代表该区域序列的肽。一旦偶联到匙孔血蓝蛋白，这种肽特异性免疫沉淀的C3抗体。该肽还抑制C3抗体对脊髓灰质炎病毒1型的中和。因此，我们得出结论，C3识别的中和表位位于衣壳多肽VP 1的氨基酸93 - 104区域内。
Using nuclease Bal31, deletions were generated within the poliovirus type 1 cDNA sequences, coding for capsid polypeptide VP1, within plasmid pCW119. The fusion proteins expressed in Escherichia coli by the deleted plasmids reacted with rabbit immune sera directed against poliovirus capsid polypeptide VP1 (alpha VP1 antibodies). They also reacted with a poliovirus type 1 neutralizing monoclonal antibody C3, but reactivity was lost when the deletion extended up to VP1 amino acids 90‐104. Computer analysis of the protein revealed a high local density of hydrophilic amino acid residues in the region of VP1 amino acids 93‐103. A peptide representing the sequence of this region was chemically synthesized. Once coupled to keyhole limpet hemocyanin, this peptide was specifically immunoprecipitated by C3 antibodies. The peptide also inhibited the neutralization of poliovirus type 1 by C3 antibodies. We thus conclude that the neutralization epitope recognized by C3 is located within the region of amino acids 93‐104 of capsid polypeptide VP1.