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人巨细胞病毒(HCMV)糖蛋白复合物Ⅱ包括两种蛋白,即糖蛋白M(gM)和糖蛋白N(gN).尽管来自于HCMV阳性病人血清中的糖蛋白复合物Ⅱ的IgG抗体能够中和HCMV粒子,但迄今为止,还没有gM中和性抗原表位的相关研究.应用消减杂交技术,通过噬菌体肽库筛选获得gM抗原的一个表位,即MAD.MAD氨基酸序列与gM第32～38位序列高度同源.将MAD与钥孔血蓝蛋白偶联免疫小鼠可产生抗MAD多抗,该多抗不仅结合天然HCMV病毒粒子,而且特异结合重组表达的gM30～78多肽.ELISA结果表明MAD能够特异结合HCMV阳性的病人血清.病毒中和实验结果进一步证明抗MAD多抗能够抑制HCMV AD169株病毒感染人胚肺细胞.总之,MAD表位有可能成为HCMV病毒疫苗潜在的保护性抗原.
Human cytomegalovirus (HCMV) glycoprotein complex II includes two proteins, glycoprotein M (gM) and glycoprotein N. (gN) Although IgG antibodies from glycoprotein complex II in the serum of HCMV-positive patients are able to Neutralization of HCMV particles, but so far no gM-neutralizing epitopes have been studied.A subtractive hybridization technique was used to obtain an epitope of gM antigen by phage display peptide library, ~ 38 sequences are highly homologous.Coupling MAD with keyhole limpet hemocyanin produces anti-MAD polyclonal antibodies that bind not only to native HCMV virions but also to recombinantly expressed gM30-78 polypeptides.ELISA The results showed that MAD could specifically bind to HCMV-positive patient serum.The results of virus neutralization further prove that anti-MAD polyclonal antibody can inhibit HCMV AD169 virus infection of human embryonic lung cells.In summary, MAD epitope may be potentially protective against HCMV virus vaccine antigen.