Chong Y H, Payne S L, Issel C J, Montelaro R C, Rushlow K E
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pennsylvania 15261.
J Virol. 1991 Feb;65(2):1007-12. doi: 10.1128/JVI.65.2.1007-1012.1991.
A panel of recombinant trpLE-gag fusion proteins and synthetic peptides was used in Western immunoblot and enzyme-linked immunosorbent assays to identify segments of the major core protein (p26) of equine infectious anemia virus that are antigenic in horses during experimental and natural infections with the virus. The predominant humoral immune response was directed toward a highly immunogenic domain composed of 83 amino acids from the carboxy terminus of p26. The observed immunogenicity of p26 resembled that reported for p24 of human immunodeficiency virus type 1, suggesting the conservation of structural motifs in the lentiviral core proteins which are responsible for their observed immunogenicity during persistent lentivirus infections.
一组重组trpLE - gag融合蛋白和合成肽被用于蛋白质免疫印迹法和酶联免疫吸附测定，以鉴定马传染性贫血病毒主要核心蛋白（p26）的片段，这些片段在马匹受到该病毒的实验性感染和自然感染期间具有抗原性。主要的体液免疫反应针对的是一个高度免疫原性的结构域，该结构域由p26羧基末端的83个氨基酸组成。观察到的p26免疫原性与报道的1型人类免疫缺陷病毒p24的免疫原性相似，这表明慢病毒核心蛋白中的结构基序具有保守性，这些结构基序在持续性慢病毒感染期间导致了它们所观察到的免疫原性。
