Escherichia Coli.
Sterile Filtered clear solution.
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
HIV-2 gp160 produced in E. coli having a Mw of 42kDa.
HIV-1 and HIV-2 exhibit differences in their RNA packaging mechanisms. While HIV-1 can bind to various RNA molecules, HIV-2 demonstrates a preference for binding to the mRNA responsible for encoding its Gag protein. This selective binding in HIV-2 contributes to its lower mutation rate compared to HIV-1. Both HIV-1 and HIV-2 share common transmission routes, primarily through contact with infected bodily fluids such as blood, semen, vaginal secretions, and tears. However, HIV-2 infection is characterized by a slower progression to immunodeficiency compared to HIV-1. In the initial stages of infection, HIV-2 exhibits lower infectivity than HIV-1; however, its infectivity increases as the disease progresses. Notable distinctions between the two viruses include the reduced pathogenicity of HIV-2, enhanced immune system control over HIV-2 infection, and a degree of independence from CD4 cells in some cases. Despite significant differences in their genetic sequences and phenotypic characteristics, the envelope proteins of HIV-1 and HIV-2 share structural similarities. Both viruses possess membrane-anchored proteins that assemble into six-helix bundles within their ectodomain regions, a common feature observed in various viral and cellular fusion proteins, which is believed to be a driving force behind membrane fusion.
The HIV2 gp160 protein encompasses the HIV2 Subtype A sequence, spanning regions C4, V5, and C5 of the HIV2 gp120 protein and extending to the HIV2 gp36 protein.
The HIV-2 gp160 protein, with a molecular weight of 42 kDa, is produced using E. coli as the expression system.
Sterile Filtered clear solution.
The HIV-2 gp160 solution is formulated to contain 25mM K2CO3, phosphate-buffered saline (PBS), and 8M urea.
For short-term storage (up to 2-4 weeks), the solution should be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein, such as 0.1% HSA or BSA, is advisable for long-term storage to enhance protein stability. Repeated freeze-thaw cycles should be avoided to maintain protein integrity.
The purity of the HIV-2 gp160 protein is determined to be greater than 90% based on analysis using 10% SDS-PAGE followed by Coomassie blue staining.
This HIV-2 gp160 protein is suitable for use in lateral flow immunoassays and enzyme-linked immunosorbent assays (ELISAs).
Escherichia Coli.
Human Immunodeficiency Virus type 2 (HIV-2) is a less common and less pathogenic strain of HIV compared to HIV-1. The envelope glycoprotein gp160 is a precursor protein that plays a crucial role in the virus’s ability to infect host cells. Recombinant gp160 (rgp160) is a synthetically produced version of this protein, often used in research and diagnostic applications.
The gp160 protein is synthesized as a polyprotein and undergoes glycosylation and proteolytic cleavage to form two subunits: gp120 and gp41 . These subunits are essential for the virus’s ability to bind to and enter host cells. The gp120 subunit is responsible for binding to the CD4 receptor on host cells, while gp41 facilitates the fusion of the viral and cellular membranes .
Producing recombinant gp160 involves expressing the protein in a host system, such as Escherichia coli, insect cells, or mammalian cells. Each system has its advantages and challenges. For instance, expressing gp160 in E. coli can be cost-effective but may require modifications to overcome issues related to hydrophobic regions and glycosylation . In contrast, insect and mammalian cells can produce more authentic versions of the protein but at a higher cost .
Recombinant gp160 is used in various applications, including:
One of the main challenges in producing recombinant gp160 is its complex structure, which includes strong hydrophobic regions and heavy glycosylation . Advances in biotechnology are continually improving the methods for producing and purifying this protein, making it more accessible for research and diagnostic purposes.
In the future, recombinant gp160 could play a significant role in the development of new diagnostic tools and vaccines, contributing to the global effort to combat HIV/AIDS.