ADDITION OF A FOREIGN OLIGOPEPTIDE TO THE MAJOR CAPSID PROTEIN OF POLIOVIRUS
ADDITION OF A FOREIGN OLIGOPEPTIDE TO THE MAJOR CAPSID PROTEIN OF POLIOVIRUS
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DOI：
10.1073/pnas.85.22.8668
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发表时间：
1988-11-01
影响因子：
11.1
通讯作者：
CANDREA, A
中科院分区：
文献类型：
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作者：
COLBEREGARAPIN, F;CHRISTODOULOU, C;CANDREA, A
构建了3型脊髓灰质炎病毒（Sabin株）的插入突变体，其在中和位点1内的衣壳多肽VP1的残基100水平编码额外的氨基酸序列，对应于衣壳表面上的环。添加三肽或六肽不会妨碍病毒活力。插入突变体的抗原模式仅局部修改：所有突变体失去了中和位点1与相应的单克隆抗体的反应性，而位点2和3的反应性不受插入的影响。我们找到了一个变种人。vFG68. sbd.中和位点1的抗原特异性被新的抗原特异性取代。尽管vFG 68与其亲本Sabin株的不同之处仅在于在VP1内添加了三个氨基酸，但天然病毒粒子以及热变性突变病毒粒子诱导了对vFG 68特异性的中和抗体。我们的研究结果表明，三个或六个氨基酸的寡肽可以延长VP1在抗原位点1的水平，而不影响病毒的繁殖，这种外来肽暴露在病毒粒子表面。
Insertion mutants of type 3 poliovirus (Sabin strain) were constructed that encode additional amino acid sequences at the level of residue 100 of the capsid polypeptide VP1 within the neutralization site 1, corresponding to a loop on the capsid surface. The addition of a tri- or hexapeptide did not hamper virus viability. The antigenic pattern of insertion mutants was only modified locally: all mutants lost reactivity of neutralization site 1 with the corresponding monoclonal antibodies, while the reactivity of sites 2 and 3 was unaffected by the insertion. We have shown for one of the mutants .sbd. vFG68 .sbd. that the antigenic specificity of the neutralization site 1 was replaced by a new one. Although vFG68 differs from its parental Sabin strain only by the addition of three amino acids within VP1, neutralizing antibodies specific for vFG68 were induced by the native virion as well as by the heat-denatured mutated virions. Our results demonstrate that an oligopeptide of three or six amino acids can lengthen VP1 at the level of antigenic site 1 without affecting virus multiplication and that this foreign peptide is exposed on the virion surface.