Van Gennip H G P, Vlot A C, Hulst M M, De Smit A J, Moormann R J M
Department of Notifiable and Exotic Viral Diseases, Central Institute of Animal Disease Control, Wageningen UR, P.O. Box 2004, 8203 AA Lelystad, The Netherlands.
J Virol. 2004 Aug;78(16):8812-23. doi: 10.1128/JVI.78.16.8812-8823.2004.
Two related classical swine fever virus (CSFV) strain Brescia clones were isolated from blood samples from an infected pig. Virus C1.1.1 is a cell-adapted avirulent variant, whereas CoBrB is a virulent variant. Sequence analysis revealed 29 nucleic acid mutations in C1.1.1, resulting in 9 amino acid substitutions compared to the sequence of CoBrB (476)R. Using reverse genetics, parts of the genomes of these viruses, which contain differences that lead to amino acid changes, were exchanged. Animal experiments with chimeric viruses derived from C1.1.1 and CoBrB (476)R showed that a combination of amino acid changes in the structural and nonstructural regions reduced the virulence of CSFV in pigs. Moreover, the presence of a Leu at position 710 in structural envelope protein E2 seemed to be an important factor in the virulence of the virus. Changing the Leu at position 710 in the CoBrB (476)S variant into a His residue did not affect virulence. However, the (710)His in the C1.1.1/CoBrB virus, together with adaptive mutations (276)R, (476)R, and (477)I in E(rns), resulted in reduced virulence in pigs. These results indicated that mutations in E(rns) and E2 alone do not determine virulence in pigs. The results of in vitro experiments suggested that a high affinity for heparan sulfate of C1.1.1 E(rns) may reduce the spread of the C1.1.1/CoBrB virus in pigs and together with the altered surface structure of E2 caused by the (710)L-->H mutation may result in a less efficient infection of specific target cells in pigs. Both these features contributed to the attenuation of the C1.1.1/CoBrB virus in vivo.
从一头感染猪的血液样本中分离出了两株相关的古典猪瘟病毒(CSFV)布雷斯西亚克隆株。病毒C1.1.1是一种细胞适应的无毒变异株,而CoBrB是一种有毒变异株。序列分析显示C1.1.1中有29个核酸突变,与CoBrB(476)R的序列相比,导致9个氨基酸替换。利用反向遗传学技术,交换了这些病毒基因组中导致氨基酸变化的部分区域。对源自C1.1.1和CoBrB(476)R的嵌合病毒进行的动物实验表明,结构区和非结构区氨基酸变化的组合降低了CSFV在猪体内的毒力。此外,结构包膜蛋白E2中第710位的亮氨酸似乎是病毒毒力的一个重要因素。将CoBrB(476)S变异株中第710位的亮氨酸替换为组氨酸残基并不影响毒力。然而,C1.1.1/CoBrB病毒中的(710)组氨酸,与E(rns)中的适应性突变(276)R、(476)R和(477)I一起,导致猪的毒力降低。这些结果表明,单独的E(rns)和E2突变并不能决定猪的毒力。体外实验结果表明,C1.1.1 E(rns)对硫酸乙酰肝素的高亲和力可能会减少C1.1.1/CoBrB病毒在猪体内的传播,并且与(710)亮氨酸→组氨酸突变引起的E2表面结构改变一起,可能导致该病毒对猪体内特定靶细胞的感染效率降低。这两个特征都导致了C1.1.1/CoBrB病毒在体内的减毒。