Martínez-Torrecuadrada J L, Casal J I
Immunología y Genética Aplicada S.A. (INGENASA), Madrid, Spain.
Virology. 1995 Jul 10;210(2):391-9. doi: 10.1006/viro.1995.1355.
Overlapping fragments of the outermost capsid protein VP2 of African horse sickness virus serotype 4 (AHSV-4) have been expressed in Escherichia coli. Horse sera from infected and vaccinated animals, rabbit sera, and mice monoclonal antibodies specific for AHSV were used to screen these fragments for antigenic regions. The screening revealed that the major antigenic domain of the AHSV-4 VP2 is localized in a central region (amino acids 200 to 413) and that both the N-terminal region (aa 1-159) and the half C-terminal region (aa 414-1060) are not immunogenic. All the fragments containing a region between amino acids 253 and 413 (fragment H) were able to elicit consistently high titers of neutralizing antibodies. The ability of several subfragments of this region to evoke neutralizing antibodies indicates the presence of several sites inside this domain. However, neutralizing antibodies in sera of horse infected or vaccinated with attenuated viruses were not absorbed by fragment H, indicating that this domain is not immunodominant in AHSV. This information might be useful in designing a subunit vaccine against AHSV infection.
非洲马瘟病毒4型（AHSV - 4）最外层衣壳蛋白VP2的重叠片段已在大肠杆菌中表达。使用来自感染和接种动物的马血清、兔血清以及对AHSV具有特异性的小鼠单克隆抗体来筛选这些片段中的抗原区域。筛选结果显示，AHSV - 4 VP2的主要抗原结构域位于中央区域（氨基酸200至413），而N端区域（氨基酸1 - 159）和C端半区域（氨基酸414 - 1060）均无免疫原性。所有包含氨基酸253至413之间区域的片段（片段H）均能持续引发高滴度的中和抗体。该区域的几个亚片段引发中和抗体的能力表明该结构域内存在多个位点。然而，感染或接种减毒病毒的马血清中的中和抗体不会被片段H吸收，这表明该结构域在AHSV中并非免疫显性。这些信息可能有助于设计针对AHSV感染的亚单位疫苗。
