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利用新型原核表达载体ｐＤＯＧ，在大肠杆菌中高效表达了人类免疫缺陷病毒１型（ＨＩＶ－１）ｇａｇ基因片段。表达载体利用λＰＲ启动子以及Ｔ７噬菌体基因１０（ｇ１０）的核糖体结合位点（ＲＢＳ）来有效起始表达基因的翻译。表达片段ＰＧ１包括ｐ１７Ｃ端１３个氨基酸、整个ｐ２４以及ｐ１５Ｎ端７４个氨基酸。与ＰＧ１相比，ＰＧ２片段不含有ｐ１７序列，并缺失了ｐ２４Ｎ端７７个氨基酸。两者的表达量均占总菌体的２０％以上。重组蛋白以包涵体形式存在，在提取包涵体后，经过一步离子柱层析，可以纯化到９０％以上的纯度。ＰＧ１可被一株抗ｐ２４的单抗特异识别，而ＰＧ２则不能。纯化的重组蛋白能与ＨＩＶ－１阳性血清发生特异反应，可以用于ＨＩＶ－１抗体检测。
The HIV-1 gag gene fragment was highly expressed in E. coli using a novel prokaryotic expression vector pDOG. The expression vector effectively initiates the translation of the expressed gene using the lambda PR promoter as well as the ribosome binding site (RBS) of the T7 phage gene 10 (g10). The expression fragment PG1 includes 13 amino acids at the p17C end, the entire p24 and 74 amino acids at the p15N end. Compared to PG1, the PG2 fragment does not contain the p17 sequence and has a deletion of 77 amino acids at the p24N end. The expression of both the total bacteria accounted for more than 20%. The recombinant protein is in the form of inclusion body. After extracting the inclusion body, it can be purified to over 90% purity by one-step ion-column chromatography. PG1 was specifically recognized by an anti-p24 mAb, while PG2 did not. The purified recombinant protein can react specifically with HIV-1 positive serum and can be used for HIV-1 antibody detection.