Functional role of human immunodeficiency virus type 1 vpu.

Resistance mechanism of human immunodeficiency virus type-1 protease to inhibitors: A molecular dynamic approach

Human immunodeficiency virus type 1 (HIV-1) protease inhibitors comprise an important class of drugs used in HIV treatments. However, mutations of protease genes accelerated by low fidelity of reverse transcriptase yield drug resistant mutants of reduced affinities for the inhibitors. This problem is considered to be a serious barrier against HIV treatment for the foreseeable future. In this st...

Quantification Analysis of Dot Blot Assays for Human Immunodeficiency Virus Type 1 and 2 Antibodies

Objective Dot Blot (DB) assay provides highly specific results, but usually not reliable for quantification of antibody production. The need for a more objective DB assay to provide a better definition of the immune status, against HIV antigens, promoted this study to be done to develop a quantitative DB assay. Material and Methods Dot blot (DB) strips for antibodies directed to human immuno...

Analysis of the human immunodeficiency virus type 1 M group Vpu domains involved in antagonizing tetherin

Zoonosis of chimpanzee simian immunodeficiency virus cpz to humans has given rise to both pandemic (M) and non-pandemic (O, N and P) groups of human immunodeficiency virus type-1 (HIV). These lentiviruses encode accessory proteins, including Vpu, which has been shown to reduce CD4 levels on the cell surface, as well as increase virion release from the cell by antagonizing tetherin (CD317, BST2)...

human immunodeficiency virus type 1 Tat

The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retroviruses.

We have recently shown that the envelope glycoprotein of the ROD10 isolate of human immunodeficiency virus type 2 (HIV-2) has the ability to positively regulate HIV-2 viral particle release. The activity provided by the ROD10 Env was remarkably similar to that of the HIV-1 Vpu protein, thus raising the possibility that the two proteins act in a related fashion. We now show that the ROD10 Env ca...