Robertson B H, Moore D M, Grubman M J, Kleid D G
J Virol. 1983 Apr;46(1):311-6. doi: 10.1128/JVI.46.1.311-316.1983.
Iodination of intact foot-and-mouth disease virus results in the selective labeling of VP1, substantiating its exposed location on the virion. A comparison of tryptic peptides revealed that a single tyrosine-containing peptide was labeled with iodine on intact or protease-cleaved virus. The labeled peptide from intact and protease-cleaved virus was characterized by molecular weight sizing and sequence analysis. Carboxypeptidase digestion of intact VP1, limited trypsin-cleaved VP1, and VP1 purified from bacterially contaminated tissue cultures yielded carboxyterminal residues of leucine, valine-arginine, and serine-alanine, respectively. The correlation of these findings with previous data on the amino acid sequence derived from nucleotide sequencing of serotypes A12 and O1 of foot-and-mouth disease virus VP1 places the probable exposed antigenic region of VP1 in a serotype-variable region including residues 136 through 144.
完整口蹄疫病毒的碘化作用导致VP1被选择性标记,证实了其在病毒粒子上的暴露位置。胰蛋白酶肽段的比较显示,完整或经蛋白酶切割的病毒上,一个含酪氨酸的单一肽段被碘标记。通过分子量大小测定和序列分析对完整病毒和经蛋白酶切割病毒的标记肽段进行了表征。完整VP1、有限胰蛋白酶切割的VP1以及从受细菌污染的组织培养物中纯化的VP1经羧肽酶消化后,分别产生了亮氨酸、缬氨酸 - 精氨酸和丝氨酸 - 丙氨酸的羧基末端残基。这些发现与先前关于口蹄疫病毒VP1 A12和O1血清型核苷酸序列推导的氨基酸序列数据的相关性,将VP1可能的暴露抗原区域定位在一个血清型可变区域,包括第136至144位残基。