Characteristics of HIV-Tat protein transduction domain |
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Authors: | Yoon Jong-Sub Jung Yong-Tae Hong Seong-Karp Kim Sun-Hwa Shin Min-Chul Lee Dong-Gun Shin Wan-Shik Min Woo-Sung Paik Soon-Young |
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Affiliation: | Department of Microbiology, College of Medicine, The Catholic University of Korea, Seoul 137-701, Republic of Korea. |
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Abstract: | The human immunodeficiency virus type 1 (HIV-1) Tat protein transduction domain (PTD), which contains rich arginine and lysine residues, is responsible for the highly efficient transduction of protein through the plasma membrane. In addition, it can be secreted from infected cells and has the ability to enter neighboring cells. When the PTD of Tat is fused to proteins and exogenously added to cells, the fusion protein can cross plasma membranes. Recent reports indicate that the endogenously expressed Tat fusion protein can demonstrate biodistribution of several proteins. However, intercellular transport and protein transduction have not been observed in some studies. Therefore, this study examined the intercellular transport and protein transduction of the Tat protein. The results showed no evidence of intercellular transport (biodistribution) in a cell culture. Instead, the Tat fusion peptides were found to have a significant effect on the transduction and intercellular localization properties. This suggests that the HIV-1 PTD passes through the plasma membrane in one direction. |
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