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The genome and proteins of HIV (human immunodeficiency virus) have been the subject of extensive research since the discovery of the virus in 1983. [1] [2] "In the search for the causative agent, it was initially believed that the virus was a form of the Human T-cell leukemia virus (HTLV), which was known at the time to affect the human immune system and cause certain leukemias.
Continuous HIV replication results in a state of generalized immune activation persisting throughout the chronic phase. [6] Immune activation, which is reflected by the increased activation state of immune cells and release of proinflammatory cytokines , results from the activity of several HIV gene products and the immune response to ongoing ...
A schematic structure of a HIV-1 protease. The monomers are shown in green and cyan, the Asp-25 and Asp-25´ residues are shown in red, and Ile50 and Ile50´ residues linked to a water molecule are shown in purple. The HIV protease is a C2-symmetric homodimeric enzyme consisting of two 99 amino acid monomers.
This diversity is a result of its fast replication cycle, with the generation of about 10 10 virions every day, coupled with a high mutation rate of approximately 3 x 10 −5 per nucleotide base per cycle of replication and recombinogenic properties of reverse transcriptase. [96] [97] [98]
HIV/AIDS explained in a simple way HIV replication cycle After the virus enters the body, there is a period of rapid viral replication , leading to an abundance of virus in the peripheral blood. During primary infection, the level of HIV may reach several million virus particles per milliliter of blood. [ 101 ]
The HIV-1 p24 capsid protein plays crucial roles throughout the replication cycle, making it an attractive therapeutic target. Unlike the viral enzymes ( protease , reverse transcriptase and integrase ) that are currently targeted by small-molecule antiretroviral drugs, p24 capsid proteins operate through protein-protein interactions.
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