Talbot P J, Dionne G, Lacroix M
Virology Research Center, Université du Québec, Laval, Canada.
J Virol. 1988 Aug;62(8):3032-6. doi: 10.1128/JVI.62.8.3032-3036.1988.
A surface probability method was used to select a decapeptide homologous to residues 993 to 1002 of the peplomer protein E2 of murine hepatitis virus strain JHM, a neurotropic coronavirus. This sequence of amino acids corresponded to a minor peak on a hydrophilicity plot. Immunization of mice with the chemically synthesized peptide coupled to keyhole limpet hemocyanin elicited high levels of neutralizing antibody and protected against lethal virus challenge. Protection correlated with a critical level of antipeptide antibody, which could be reached after a single inoculation. These results suggest that an appropriate antibody response to a highly restricted, surface-exposed domain of this viral protein is critical in determining the outcome of infection of the central nervous system. This sequence is located in the C-terminal fifth of the E2 peplomers, between two predicted coiled-coil structures.
采用表面概率法选择了一种十肽,该十肽与嗜神经冠状病毒小鼠肝炎病毒JHM株的包膜蛋白E2的993至1002位残基同源。此氨基酸序列对应于亲水性图上的一个小峰。用与钥孔血蓝蛋白偶联的化学合成肽免疫小鼠,可引发高水平的中和抗体,并能抵御致死性病毒攻击。保护作用与抗肽抗体的临界水平相关,单次接种后即可达到该水平。这些结果表明,对该病毒蛋白高度受限的表面暴露结构域产生适当的抗体反应对于决定中枢神经系统感染的结果至关重要。该序列位于E2包膜蛋白C端的五分之一处,介于两个预测的卷曲螺旋结构之间。