摘要
M2蛋白是A型流感病毒所特有的一种结构保守的非糖基化的跨膜蛋白,主要在病毒脱壳时酸化病毒粒子的内部环境,在表面血凝素糖蛋白合成过程中作为质子通道调节高尔基体跨膜转移通道的pH。其核苷酸序列高度保守,几乎不发生变异。其25位~43位氨基酸多肽是金刚烷胺类抗流感病毒药物的作用靶位,氨基酸极小变异都可能导致流感病毒抗药性的产生。M2蛋白胞外区域的氨基酸残基多肽（M2e）的特异性抗体可以在感染流感病毒的动物血清中检测出来,将M2e与相关佐剂联合使用可极大的提高机体对流感病毒的免疫力,在病毒感染中起重要作用,是一种潜在的交叉保护性抗原,常被用来探索具有广谱性和持久性的流感＂通用疫苗＂。
The matrix protein 2 of influenza A virus, being a integral non-glycosylated transmembrane protein, is highly conserved in amino acids. M2 regulates the vesicular pH in the infected cell, preventing the low pH-induced conformational change of haemagglutinin molecule occurring during its maturation in the trans Golgi. The amino acids of M2 have undergone remarkably little structural variation. The transmembrane portion of M2（amino acids 25 to 43） has been identified as the target of the antiviral drug amantadine, even a single amino acid change in this domain can cause a virus resistant to the drug. The ectodomain of the M2-protein of influenza A （M2e）, its specific antibodies can be detected in sera, when used either for parenteral injection or for intranasal administration in combination with a potent mucosal adjuvant, can activate a variety of immune cells, like macrophages, B-cells, and T-cells, which promises to be an interesting candidate for a universal influenza A vaccine.
出处
《动物医学进展》
CSCD
2007年第7期56-60,共5页
Progress In Veterinary Medicine
基金
国家"973"计划资助项目(2005CB523202)
