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From Proteopedia
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J. Virol. May 2010 vol. 84 no. 10 5181-5190]</ref> | J. Virol. May 2010 vol. 84 no. 10 5181-5190]</ref> | ||
| - | * Nuclear pore (certainly but not sure) | + | * Nuclear pore (certainly but not sure)<ref>[http://www.google.fr/url?sa=t&rct=j&q=&esrc=s&source=web&cd=1&ved=0ahUKEwiV2fr01MzKAhWLhhoKHafGDaUQFggiMAA&url=http%3A%2F%2Fwww.nature.com%2Fnrmicro%2Fjournal%2Fv13%2Fn8%2Ffull%2Fnrmicro3503.html&usg=AFQjCNHxI2ZQfqG9K9oGRGsoomYd40gcgw HIV-1 capsid: the multifaceted key player in HIV-1 infection Nature Reviews Microbiology 13,471–483 (2015)doi:10.1038/nrmicro3503]</ref> |
* Dynein | * Dynein | ||
* Integrase ? | * Integrase ? | ||
Revision as of 13:59, 28 January 2016
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Contents |
Introduction
Function
Structural highlights
As you can see on the figure bellow, each monomer of capsid is linked to five others to form a hexamer. These hexamers (approximately 330 per virus) associates themselves to form a non-symetrical protein complex.
Interactions with others partners
Even if p24 is classified as a structural protein, it is also involved in many cellular infection processes.
You can find bellow in a non exhaustive list of p24 partners :
- Cyclophylin A [3]
- Nuclear pore (certainly but not sure)[4]
- Dynein
- Integrase ?
The HIV-1 capsid acts like a kind of "nuclear localisation signal" because it targets directly the virus toward the nucleus, where the integration takes place.
Capsid as therapeutical target
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Thank to its central role in viral infectious process (genome protection, enveloppe cohesion, uncoating, budding), HIV capsid is a very good target for antiviral drugs. As a result, many research teams are working in this way and some molecules such as PF-3450074 are very promising. By binding to a "central pocket" on P24, it was shown in vitro that this compound is inhibiting the new viruses assembly, and consequently the virus budding.
References
- ↑ Fernandez J, Gärtner K, Becker A, et al. HIV-1 capsid interacts with cytoskeletal-associated proteins for intracytoplasmic routing to the nucleus. Retrovirology. 2013;10(Suppl 1):P34. doi:10.1186/1742-4690-10-S1-P34.
- ↑ Fernandez J, Portilho DM, Danckaert A, Munier S, Becker A, Roux P, Zambo A, Shorte S, Jacob Y, Vidalain PO, Charneau P, Clavel F, Arhel NJ. Microtubule-associated proteins 1 (MAP1) promote human immunodeficiency virus type I (HIV-1) intracytoplasmic routing to the nucleus. J Biol Chem. 2015 Feb 20;290(8):4631-46. doi: 10.1074/jbc.M114.613133. Epub 2014 Dec 11.
- ↑ [http://jvi.asm.org/content/84/10/5181.long Marisa S. Briones, Charles W. Dobard and Samson A. Chow. Role of Human Immunodeficiency Virus Type 1 Integrase in Uncoating of the Viral Core. Accepted manuscript posted online 10 March 2010, doi:.1128/JVI.02382-09 J. Virol. May 2010 vol. 84 no. 10 5181-5190]
- ↑ HIV-1 capsid: the multifaceted key player in HIV-1 infection Nature Reviews Microbiology 13,471–483 (2015)doi:10.1038/nrmicro3503
Structural capsid image : By Thomas Splettstoesser (www.scistyle.com) (Own work) [CC BY-SA 4.0 (http://creativecommons.org/licenses/by-sa/4.0)], via Wikimedia Commons
Nuclear import :
HIV-1 capsid: the multifaceted key player in HIV-1 infection Nature Reviews Microbiology 13,471–483 (2015)doi:10.1038/nrmicro3503
Capsid targeting drug
Edward M. Campbell & Thomas J. Hope. HIV-1 capsid: the multifaceted key player in HIV-1 infection Nature Reviews Microbiology 13,471–483 (2015)doi:10.1038/nrmicro3503 Published online 16 July 2015

