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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.
P24 is a structural protein that plays a crucial role in the formation and stability of the viral capsid, which protects the viral RNA. p24 capsid protein's roles in the HIV replicative process are summarized as follows: [citation needed] Fusion: HIV replication cycle begins when HIV fuses with the surface of the host cell.
Research has shown (for both same-sex and opposite-sex couples) that HIV is not contagious during sexual intercourse without a condom if the HIV-positive partner has a consistently undetectable viral load. [5] [6] HIV infects vital cells in the human immune system, such as helper T cells (specifically CD4 + T cells), macrophages, and dendritic ...
Diagram of an HIV virion structure Scanning electron micrograph of HIV-1, colored green, budding from a cultured lymphocyte. HIV is the cause of the spectrum of disease known as HIV/AIDS. HIV is a retrovirus that primarily infects components of the human immune system such as CD4 + T cells, macrophages and dendritic cells.
HIV-1 protease labelled according to its resemblance to an English Bulldog or a fat cat. [7] The blue and cyan-green ribbons depict the peptide backbone of a wild-type ( ) and a mutant ( ) structure, respectively. Mature HIV protease exists as a 22 kDa homodimer, with each subunit made up of 99 amino acids. [1]
These studies found that >95% of CD4 T cells die because of abortive HIV infection. [9] These dying cells are resting and thus are nonpermissive for productive HIV infection. Full viral replication was limited to the ~5% of activated CD4 T cells present in these tissues; these cells die by apoptosis. [10]
The positive transcription elongation factor, P-TEFb, is a multiprotein complex that plays an essential role in the regulation of transcription by RNA polymerase II (Pol II) in eukaryotes. [1] Immediately following initiation Pol II becomes trapped in promoter proximal paused positions on the majority of human genes (Figure 1).
Contains a characteristic elongated β- sheet ectodomain structure that refolds to give a trimer of hairpins. Examples of class II viral fusion proteins include the dengue virus E protein, and the west nile virus E protein. [5] [6] Class III: Structural conformation is a combination of features from Class I and Class II viral membrane fusion ...