Saiz J C, Gonzalez M J, Borca M V, Sobrino F, Moore D M
Molecular Biology Laboratory, Plum Island Animal Disease Center, U.S. Department of Agriculture, Greenport, New York 1194-0848.
J Virol. 1991 May;65(5):2518-24. doi: 10.1128/JVI.65.5.2518-2524.1991.
Five neutralizing monoclonal antibodies (nMAbs) obtained against type A5 Spain-86 foot-and-mouth disease virus were used to generate a series of neutralization-resistant variants. In vitro and in vivo assays showed that the variants were fully refractory to neutralization by the selecting nMAb. On the basis of cross-neutralization and binding assays, two neutralizing antigenic sites have been located on the virus surface; one, located near the C-terminus of VP1, displayed a linear epitope, and the second, located on VP2, displayed two conformational epitopes. Nucleotide sequencing of RNA of the parental and variant capsid protein-coding region P1 has placed the amino acid changes at position 198 of VP1 for the first site and at positions 72 and 79 of VP2 for the related epitopes in the second site. The relative importance of these two sites in the biological properties of foot-and-mouth disease virus is discussed.
针对A5型西班牙-86口蹄疫病毒获得的5种中和性单克隆抗体(nMAb)被用于产生一系列抗中和变异体。体外和体内试验表明,这些变异体对筛选出的nMAb完全具有中和抗性。基于交叉中和及结合试验,已在病毒表面定位了两个中和性抗原位点;一个位于VP1的C末端附近,呈现线性表位,另一个位于VP2上,呈现两个构象表位。亲本病毒和变异体衣壳蛋白编码区P1的RNA核苷酸测序已确定,第一个位点的氨基酸变化位于VP1的第198位,第二个位点相关表位的氨基酸变化位于VP2的第72位和第79位。本文讨论了这两个位点在口蹄疫病毒生物学特性中的相对重要性。