ENGINEERING STABLE PROT¬¬¬EINS Stable and soluble HIV spike proteins
Appendix
Abstract……………………………….................................................1
Introduction………………………………..........................................1
Structure and function of gp120 and gp41.…………………………2
Mutation 1……………………………….............................................5
Mutation 2.……………………………................................................6
Mutation 3.……………………………................................................7
Conclusions…………………………………………………………...9
References……………………………….............................................9
Abstract
The functional unit of the human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins consist of compact trimers of noncovalently associated gp120 exterior glycoproteins and gp41 transmembrane glycoproteins.The glycoproteins so called spikes have the role in virus-cell attachment and is of particular importance and is the major target for vaccine design. The lability of intersubunit interactions has hindered the production and characterization of soluble and stable forms of envelope glycoprotein trimers. Here I describe the generation of soluble and stabilized HIV-1 spike proteins by protein engineering.
Introduction
The HIV infection in humans is considered pandemic by WHO and an infection with HIV occurs by the transfer of blood, breast milk and vaginal-fluid. The virus was discovered 1983 by Luc Montagnier which he received the Nobel price 2008 for.
Human immunodeficiency virus type 1 is a lentivirus. Lentivirus is characterized by being slow and a long incubation period. They can deliver a significant amount of genetic information into the DNA of the host cell and have the unique ability among retroviruses of being able to replicate in non-dividing cells (2). HIV infects
References: 5. Forsel MN, Schief WR, Wyatt RT. Immunogenicity of HIV-1 envelope glycoprotein oligomers. 2009 Curr Opin HIV AIDS 4:380 6 11. Zhou T, Xu L, Dey B, et al. (2007). "Structural definition of a conserved neutralization epitope on HIV-1 gp120". Nature 445 (7129): 732-737.