Pulli T, Roivainen M, Hovi T, Hyypiä T
Enterovirus Laboratory, National Public Health Institute, Helsinki, Finland. timo@
J Gen Virol. 1998 Sep;79 ( Pt 9):2249-53. doi: 10.1099/0022-1317-79-9-2249.
The arginine-glycine-aspartic acid motif at the C terminus of coxsackievirus A9 capsid protein VP1 has been shown to play a role in specific attachment of the virus to alpha(v)beta3 integrin on the host cell surface. The C-terminal region of the VP1 protein has also been shown to be highly antigenic by using peptide scanning techniques. To find out whether this region contains a neutralizing epitope, three overlapping peptides covering the C-terminal end of VP1 were synthesized and rabbit antisera were raised against these peptides. Neutralization of the virus was observed with all three antipeptide antisera in A549 cells and with two antisera in RD cells.
柯萨奇病毒A9衣壳蛋白VP1 C末端的精氨酸-甘氨酸-天冬氨酸基序已被证明在病毒与宿主细胞表面α(v)β3整合素的特异性结合中发挥作用。通过肽扫描技术也已证明VP1蛋白的C末端区域具有高度抗原性。为了确定该区域是否包含中和表位，合成了覆盖VP1 C末端的三个重叠肽，并制备了针对这些肽的兔抗血清。在A549细胞中，所有三种抗肽抗血清均观察到病毒中和作用，在RD细胞中，两种抗血清观察到病毒中和作用。
