删除猪圆环病毒 2 型 Cap 蛋白的单一潜在 N-糖基化位点通过 DNA 免疫增强小鼠的特异性免疫反应。
Deletion of the single putative N-glycosylation site of the porcine circovirus type 2 Cap protein enhances specific immune responses by DNA immunisation in mice.
机构信息
Key Laboratory of Animal Diseases Diagnostic and Immunology, Ministry of Agriculture, College of Veterinary Medicine, Nanjing Agriculture University, Nanjing 210095, Jiangsu, China.
出版信息
Vet J. 2012 Jun;192(3):385-9. doi: 10.1016/j.tvjl.2011.08.005. Epub 2011 Oct 19.
The immunogenicity of a putative N-linked glycosylation site located at amino acids 143-145 (N143YS) of the porcine circovirus 2 (PCV2) Cap protein was investigated. Eukaryotic vectors expressing wild-type PCV2 Cap (pCap) and N-linked glycosylation site mutant Cap (pCap-m) were constructed and the immunogenicity of these proteins was determined following DNA vaccination in BALB/c mice. pCap-m elicited significantly higher Cap-specific T lymphocyte proliferative activity, percentage of CD8(+) T cells, ratio of immunoglobulin (Ig) G2a:IgG1 and levels of interferon-γ compared to pCap (P<0.05). These results indicate that deletion of the N-glycosylation site in the PCV2 Cap protein enhances specific immune responses and may have a role in Cap-based DNA vaccines with enhanced immunogenicity.
本研究旨在探究位于猪圆环病毒 2（PCV2）衣壳蛋白氨基酸 143-145 处（N143YS）的一个假定 N 连接糖基化位点的免疫原性。构建了表达野生型 PCV2 衣壳蛋白（pCap）和 N 连接糖基化位点突变衣壳蛋白（pCap-m）的真核载体，并在 BALB/c 小鼠中进行 DNA 疫苗接种后，测定这些蛋白的免疫原性。与 pCap 相比，pCap-m 诱导的 Cap 特异性 T 淋巴细胞增殖活性、CD8(+)T 细胞百分比、IgG2a:IgG1 比值和干扰素-γ水平显著更高（P<0.05）。这些结果表明，PCV2 衣壳蛋白中 N 糖基化位点的缺失增强了特异性免疫反应，并且可能在增强免疫原性的基于 Cap 的 DNA 疫苗中发挥作用。
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