Li Q, Yafal A G, Lee Y M, Hogle J, Chow M
Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock 72205.
J Virol. 1994 Jun;68(6):3965-70. doi: 10.1128/JVI.68.6.3965-3970.1994.
Antisera were raised against peptide sequences that are normally internal in the poliovirus virion. These antisera contain neutralizing activity, but this neutralizing activity is dependent on coincubation of the virus and antisera at 37 degrees C. Immunoprecipitation analyses demonstrate that the neutralization is due to exposure of these normally internal sequences at 37 degrees C and subsequent antibody binding. Exposure of these sequences is reversible. These data demonstrate that the poliovirus particle is a dynamic entity that is capable of undergoing conformational alterations at physiological temperatures. This conformational flexibility provides an explanation for earlier observations of virus neutralization by antibodies to internal epitopes which can be accommodated within the framework of existing models for antibody-mediated neutralization of viral infectivity. Analogies between the sequences which are reversibly exposed at 37 degrees C with those which are irreversibly exposed upon receptor binding suggest that the observed conformational dynamics also may play a role in cell entry.
制备了针对脊髓灰质炎病毒病毒粒子中通常位于内部的肽序列的抗血清。这些抗血清具有中和活性，但这种中和活性依赖于病毒和抗血清在37℃下共同孵育。免疫沉淀分析表明，中和作用是由于这些通常位于内部的序列在37℃下暴露并随后与抗体结合所致。这些序列的暴露是可逆的。这些数据表明，脊髓灰质炎病毒粒子是一个动态实体，能够在生理温度下发生构象改变。这种构象灵活性为早期观察到的针对内部表位的抗体介导的病毒中和现象提供了解释，这一现象可以在现有的抗体介导的病毒感染性中和模型框架内得到解释。在37℃下可逆暴露的序列与受体结合后不可逆暴露的序列之间的相似性表明，观察到的构象动力学也可能在细胞进入过程中起作用。
