Gething M J, Sambrook J
Nature. 1982 Dec 16;300(5893):598-603. doi: 10.1038/300598a0.
The DNA sequences encoding the amino-terminal signal peptide or the carboxy-terminal hydrophobic anchor have been deleted from a cloned gene coding for the haemagglutinin (HA) of influenza virus. The wild-type gene has previously been shown to be expressed with high efficiency from simian virus 40 (SV40)-HA recombinant vectors into a fully glycosylated protein that is displayed on the infected cell's surface in an antigenically and biologically active form. The anchor-minus HA also is glycosylated but is secreted efficiently into the medium. By contrast, the signal-minus HA is produced only at low levels, is not glycosylated and is located intracellularly.
编码流感病毒血凝素（HA）的克隆基因中，编码氨基末端信号肽或羧基末端疏水锚定序列已被删除。野生型基因先前已被证明能从猿猴病毒40（SV40）-HA重组载体高效表达为一种完全糖基化的蛋白质，该蛋白质以抗原性和生物活性形式展示在受感染细胞的表面。缺失锚定序列的HA也能被糖基化，但能有效分泌到培养基中。相比之下，缺失信号肽的HA仅以低水平产生，未被糖基化且位于细胞内。
