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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.
The p24 capsid protein is the most abundant HIV protein with each virus containing approximately 1,500 to 3,000 p24 molecules. [1] It is the major structural protein within the capsid , and it is involved in maintaining the structural integrity of the virus and facilitating various stages of the viral life cycle, including viral entry into host ...
Two types of HIV have been characterized: HIV-1 and HIV-2. HIV-1 is the virus that was initially discovered and termed both lymphadenopathy associated virus (LAV) and human T-lymphotropic virus 3 (HTLV-III). HIV-1 is more virulent and more infective than HIV-2, [20] and is the cause of the majority of HIV infections globally. The lower ...
A 3D representation that includes the retroviral psi packaging element. This is a solution RNA structure model of the HIV-1 dimerization initiation site in the kissing-loop dimer. [7] In HIV, the psi element is around 80–150 nucleotides in length, and located at the 5' end of the genome just upstream of the gag initiation codon. [8]
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.
Since CD4 receptor binding is the most obvious step in HIV infection, gp120 was among the first targets of HIV vaccine research. Efforts to develop HIV vaccines targeting gp120, however, have been hampered by the chemical and structural properties of gp120, which make it difficult for antibodies to bind to it. gp120 can also easily be shed from the surface of the virus and captured by T cells ...
HIV MA also makes contacts with the HIV trans-membrane glycoprotein gp41 in the assembled virus and, indeed, may have a critical role in recruiting Env glycoproteins to viral budding sites. [citation needed] Once Gag is translated on ribosomes, Gag polyproteins are myristoylated at their N-terminal glycine residues by N-myristoyltransferase 1 ...
[1] [2] HIV-1 PR cleaves newly synthesized polyproteins (namely, Gag and Gag-Pol [3]) at nine cleavage sites to create the mature protein components of an HIV virion, the infectious form of a virus outside of the host cell. [4] Without effective HIV-1 PR, HIV virions remain uninfectious. [5] [6]