Sandbox Reserved 1741: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 4: Line 4:


== Function ==
== Function ==
HIV is a retrovirus, which means that it only carries single stranded RNA, and so relies on reverse transcription to propagate itself to new cells (1).  HIV reverse transcriptase (RT) is a heterodimer consisting of a p51 and a p66 subunit, the latter of which contains catalytically active DNA polymerase and RNase H domains, essentially functioning as a catalyst for the reverse transcription reaction (2).  The enzyme RT is responsible for turning the infectious single-stranded ssRNA genome into double-stranded dsDNA provirus to integrate the virus into a new host cell (3).  HIV integrase then integrates it into the host chromosome.  The retro transcription process begins when the HIV particle fuses with the membrane of the host due to interactions between the envelope of the glycoprotein and coreceptors on the surface of the host cell (4).  The infectious content of the HIV particle is then released into the cytoplasm of the host cell.  Here the ssRNA serves as a template for HIV RT to form the dsDNA provirus.  The dsDNA is then imported into the nucleus, which is then integrated into the host chromosome by another enzyme, HIV integrase.  Once the dsDNA is integrated into the nucleus it makes modified mRNA that code for viral proteins and new ssRNA gnomes that combine to form new viral HIV particles (3).  The process then repeats as the new viral particles target uninfected host cells.
HIV is a retrovirus, which means that it only carries single stranded RNA, and so relies on reverse transcription to propagate itself to new cells (1).  HIV reverse transcriptase (RT) is a heterodimer consisting of a p51 and a p66 subunit, the latter of which contains catalytically active DNA polymerase and RNase H domains, essentially functioning as a catalyst for the reverse transcription reaction (2).  The enzyme RT is responsible for turning the infectious single-stranded ssRNA genome into double-stranded dsDNA provirus to integrate the virus into a new host cell (3).  HIV integrase then integrates it into the host chromosome.  The retro transcription process begins when the HIV particle fuses with the membrane of the host due to interactions between the envelope of the glycoprotein and coreceptors on the surface of the host cell (4).  The infectious content of the HIV particle is then released into the cytoplasm of the host cell.  Here the ssRNA serves as a template for HIV RT to form the dsDNA provirus.  The dsDNA is then imported into the nucleus, which is then integrated into the host chromosome by another enzyme, HIV integrase.  Once the dsDNA is integrated into the nucleus it makes modified mRNA that code for viral proteins and new ssRNA gnomes that combine to form new viral HIV particles (3).  Some viral proteins that are made by the modified mRNA include Gag, Gag-Pol, and Env.  The modified mRNA also codes for the new accessory proteins Nef, Vif, Vpr, and Vpu. (8)  These viral proteins then form chains, which combine with the ssRNA to form new viral particles.  These particles then release (bud) from the cell, taking some of the cell membrane with it. (8)  The viral particles seek out new host cells to infect, spreading the virus through the system and starting the process anew.


[[Image:2022-11-27 (30).png]]
[[Image:2022-11-27 (30).png]]
Line 48: Line 48:
(7) Jacobo-Molina, A.; Arnold, E. Perspectives in Biochemistry: HIV Reverse Transcriptase Structure-Function Relationships. Biochem. 1991, 30 (26), 6351-6361.
(7) Jacobo-Molina, A.; Arnold, E. Perspectives in Biochemistry: HIV Reverse Transcriptase Structure-Function Relationships. Biochem. 1991, 30 (26), 6351-6361.


Sluis-Cremer, N.; Tachedjian, G. Mechanisms of Inhibition of HIV Replication by Non-
(8) Sluis-Cremer, N.; Tachedjian, G. Mechanisms of Inhibition of HIV Replication by Non-
Nucleoside Reverse Transcriptase Inhibitors. ''Virus Research'' '''2008''', ''134'' (1-2), 147–156.
Nucleoside Reverse Transcriptase Inhibitors. ''Virus Research'' '''2008''', ''134'' (1-2), 147–156.