| Expression and Characterization of Human Immunodeficiency Virus-1 Oligomerized gp140 Protein in Mammalian Cells |
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Eun-Ok Kim, Eun Kim, Hyun-Soo Kim, Kwang-Soon Shin, Chul-Joong Kim |
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College of Veterinary Medicine, Chungnam National University |
| 포유동물 세포에서 Human Immunodeficiency Virus-1의 Oligomeric gp140 단백의 발현 및 특성 |
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김은옥, 김은, 김현수, 신광순, 김철중 |
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충남대학교 수의과대학 |
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| Abstract |
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The envelope glycoprotein of HIV-1 forms an oligomeric complex resulting in playing a role to induce neutralizing antibody and cell-mediate immune responses. The oligomer exists as a trimer of gp120-gp41 heterodimer which mediates HIV-1 attachment and fusion. We made a cDNA clone of gp140 consisting of gp120 and ectodomain of gp41 from the primary African isolate. To express the oligomeric gp140 in mammalian cells, we adopted the Semliki Forest virus (SFV) based expression system. The oligomeric gp140 in the secretory form was expressed and purified from the cell culture supernatant and characterized. The antibody inducing activity of the purified gp140 was also examined in mice inoculation. |
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