Hunt A R, Johnson A J, Roehrig J T
Division of Vector-Borne Infectious Diseases, Centers for Disease Control, Fort Collins, Colorado 80522.
Virology. 1990 Dec;179(2):701-11. doi: 10.1016/0042-6822(90)90137-g.
Fourteen peptides representing 67% of the extramembranal domain of the Venezuelan equine encephalomyelititis (VEE) virus E2 glycoprotein were synthesized and analyzed to determine their antigenic, immunogenic, and protective capacities. Thirteen of 14 peptides elicited antibody for the homologous peptide. Thirteen peptides elicited antiviral antibody that recognized either the Trinidad (TRD) strain of VEE virus or the TC-83 vaccine derivative, or both. Two peptides, VE2pep01(TC-83) and VE2pep01(TRD), protected significant numbers of mice from TRD virus challenge. The majority of the peptides were reactive with antisera from mice immunized with the various subtypes of VEE virus. A competition assay using antipeptide antibodies to block virus binding of anti-VEE virus monoclonal antibodies corroborated previous studies on the spatial relationship of E2 epitopes and provided evidence for a spatial overlap of the E2 amino terminus with a domain composed of residues 180-210.
合成并分析了代表委内瑞拉马脑炎(VEE)病毒E2糖蛋白膜外结构域67%的14种肽,以确定它们的抗原性、免疫原性和保护能力。14种肽中的13种引发了针对同源肽的抗体。13种肽引发了抗病毒抗体,该抗体可识别VEE病毒的特立尼达(TRD)毒株或TC-83疫苗衍生物,或两者皆可识别。两种肽,VE2pep01(TC-83)和VE2pep01(TRD),保护了大量小鼠免受TRD病毒攻击。大多数肽与用VEE病毒各种亚型免疫的小鼠的抗血清发生反应。使用抗肽抗体阻断抗VEE病毒单克隆抗体的病毒结合的竞争试验证实了先前关于E2表位空间关系的研究,并为E2氨基末端与由残基180 - 210组成的结构域的空间重叠提供了证据。