Johnson A J, Hunt A R, Roehrig J T
Division of Vector-Borne Infectious Diseases, Centers for Disease Control, Fort Collins, Colorado 80522.
Virology. 1991 Dec;185(2):840-2. doi: 10.1016/0042-6822(91)90555-p.
To complete our analysis of the E2 glycoprotein of Venezuelan equine encephalomyelitis (VEE) virus, we prepared six synthetic peptides corresponding to the extramembranal carboxy-terminal one-third of the protein. NIH-Swiss mice were immunized with the peptides, and antipeptide and antiviral titers were determined by enzyme-linked immunosorbent assay (ELISA). Challenge studies revealed that peptide 13 (amino acids 241-265) protected 60-70% of virus-challenged mice. Although the other peptides generally elicited antipeptide ELISA titers but no or low antiviral titers and did not protect mice, significant E2 reactivity was found in immunoblots. These results provide the first direct evidence that much of the E2 carboxy-terminal domain is cryptic in the VEE virion, even when virus was bound to polystyrene ELISA plates.
为完成对委内瑞拉马脑炎（VEE）病毒E2糖蛋白的分析，我们制备了6种对应于该蛋白膜外羧基末端三分之一区域的合成肽。用这些肽对NIH - 瑞士小鼠进行免疫，并通过酶联免疫吸附测定（ELISA）确定抗肽和抗病毒效价。攻毒研究表明，肽13（氨基酸241 - 265）可保护60 - 70%受病毒攻击的小鼠。虽然其他肽通常能引发抗肽ELISA效价，但无抗病毒效价或效价较低，且不能保护小鼠，但在免疫印迹中发现了显著的E2反应性。这些结果提供了首个直接证据，即即便病毒结合在聚苯乙烯ELISA板上，VEE病毒粒子中E2羧基末端的大部分区域仍是隐蔽的。
