HIV-1, 2 recombinant- E.Coli derived recombinant 27 kDa protein contains the C- terminus of gp120 and most of gp41. The protein is conjugated to a 23 amino acids synthetic peptide derived from gp39 of HIV-2.
Specificity
Immunoreactive with all sera of HIV-1, HIV type O & HIV-2 infected individuals.
Nature
Recombinant
Tag/Conjugate
Unconjugated
Alternative Names
Human Immunodeficiency Virus; HIV gp41; HIV; HIV-1 gp41; HIV-1; HIV type 1 gp41; HIV-1 gp120; HIV-1 envelope
Purity
Greater than 95.0% as determined by HPLC analysis and SDS-PAGE.
Format
Liquid
Buffer
100mM NaPO4, pH 6 and 0.05% SDS
Preservative
None
Storage
HIV-1,2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Introduction
HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids.Immunodeficiency develops more slowly with HIV-2.HIV-2 is less infectious in the early stages of the virus than with HIV-1.The infectiousness of HIV-2 increases as the virus progresses.Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion.HIV-1 gp41 helical regions can form more stable 6-helix bundles than HIV-2 gp41 helical regions however HIV-2 fusion occurs at a lower threshold temperature (25°C), does not require Ca2+ in the medium, is insensitive to treatment of target cells with cytochalasin B, and is not affected by target membrane glycosphingolipid composition.
Keywords
Human Immunodeficiency Virus; HIV gp41; HIV; HIV-1 gp41; HIV-1; HIV type 1 gp41; HIV-1 gp120; HIV-1 envelope
Citations
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Background
Two of the most common HIV viruses are HIV-1 and HIV-2 – two virus that are totally different in structure and function. HIV-1's envelope glycoprotein gp41 is among the proteins involved in the entry of the virus into host cells. It mostly allows the virus and the cell membrane to fuse. When gp41 comes into contact with the target cell, it changes its shape by binding to the CD4 receptor and co-receptors (CCR5 or CXCR4) and then showing its transmembrane tail, which makes the virus fuse to the membrane of the host cell. Its conformational change includes an apparent conformational shift in the N-terminal region of gp41, which becomes significantly altered upon contact with CD4, showing its HR1 and HR2 domains and a six-helix bundle arrangement that induces fusion with the host cell membrane. Research revealed that gp41's amino acid sequence was conserved among HIV-1 variants, including its V1/V2 variable loop region, which is of particular interest to antiviral drugs and antibodies. Additionally, antibodies to gp41 can identify and eliminate most HIV-1 variants, thus making it a key target for viral immune escape.
Another major HIV-1 glycoprotein, gp120, also binds to the CD4 receptor, and it enters host cells via its co-receptors. Gp120 also includes a handful of highly variable domains (V1-V5) that virus can slip inside so the host immune system might not detect it. In the case of gp120, it turns out that its V3 loop region is especially receptive to antibody, making it an attractive target for vaccines. During the viral life cycle, gp120 forms a stable trimeric complex with gp41, anchored on the virus surface through non-covalent interactions. This structure not only supports the virus's fusion mechanism but also influences its recognition and invasion of host cells.
Figure 1. HIV-1 viral entry (Source: Chen B. 2019)
The envelope glycoprotein gp36 of HIV-2 shares some things with the envelope glycoproteins gp120 and gp41 of HIV-1. In experiments, HIV-2 gp36 looks similar to HIV-1 gp120 and gp41, respectively, both in structure and function, when it comes to ensnaring the virus on the host cell. But the amino acid sequence of HIV-2's envelope glycoprotein varies greatly, and this can alter antigenicity and resistance to immune attack. There is currently little definite structural data on HIV-2 gp36, but it has been hypothesized that the V3 loop area of the protein could have valuable antigenic properties. Additionally, the envelope glycoproteins of HIV-2 exhibit some polymorphism among different variants, which may be related to their transmission and adaptability in various populations.
References
1. Chen B. Molecular Mechanism of HIV-1 Entry. Trends Microbiol. 2019 Oct;27(10):878-891.
2. Chiodi F, et al. Antigenic and immunogenic sites of HIV-2 glycoproteins. Chem Immunol. 1993;56:61-77.
3. Valadés-Alcaraz A, et al. HIV Transmembrane Glycoprotein Conserved Domains and Genetic Markers Across HIV-1 and HIV-2 Variants. Front Microbiol. 2022 May 27;13:855232.
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References
A Helical Short-Peptide Fusion Inhibitor with Highly Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus
Human immunodeficiency virus type 2 (HIV-2) has already spread to different regions worldwide, and currently about 1 to 2 million people have been infected, calling for new antiviral agents that are effective on both HIV-1 and HIV-2 isolates. T20 (enfuvirtide), a 36-mer peptide derived from the C-terminal heptad repeat region (CHR) of gp41, is the only clinically approved HIV-1 fusion inhibitor, but it easily induces drug resistance and is not active on HIV-2. In this study, we first demonstrated that the M-T hook structure was also vital to enhancing the binding stability and inhibitory activity of diverse CHR-based peptide inhibitors. We then designed a novel short peptide (23-mer), termed 2P23, by introducing the M-T hook structure, HIV-2 sequences, and salt bridge-forming residues. Promisingly, 2P23 was a highly stable helical peptide with high binding to the surrogate targets derived from HIV-1, HIV-2, and simian immunodeficiency virus (SIV). Consistent with this, 2P23 exhibited potent activity in inhibiting diverse subtypes of HIV-1 isolates, T20resistant HIV-1 mutants, and a panel of primary HIV-2 isolates, HIV-2 mutants, and SIV isolates. Therefore, we conclude that 2P23 has high potential to be further developed for clinical use, and it is also an ideal tool for exploring the mechanisms of HIV-1/2-and SIV-mediated membrane fusion. IMPORTANCE The peptide drug T20 is the only approved HIV-1 fusion inhibitor, but it is not active on HIV-2 isolates, which have currently infected 1 to 2 million people and continue to spread worldwide. Recent studies have demonstrated that the M-T hook structure can greatly enhance the binding and antiviral activities of gp41 CHR-derived inhibitors, especially for short peptides that are otherwise inactive. By combining the hook structure, HIV-2 sequence, and salt bridge-based strategies, the short peptide 2P23 has been successfully designed. 2P23 exhibits prominent advantages over many other peptide fusion inhibitors, including its potent and broad activity on HIV-1, HIV-2, and even SIV isolates, its stability as a helical, oligomeric peptide, and its high binding to diverse targets. The small size of 2P23 would benefit its synthesis and significantly reduce production cost. Therefore, 2P23 is an ideal candidate for further development, and it also provides a novel tool for studying HIV-1/2-and SIV-mediated cell fusion.
Immobilization of HIV GP41 antibodies on glass substrates for HIV biosensing
FRONTIERS IN BIOLOGICAL DETECTION: FROM NANOSENSORS TO SYSTEMS XII
Biological macromolecules such as antibodies, enzymes, proteins and aptamers have good molecular recognition ability which makes them good candidates for biosensing applications. In this study, glass substrates were treated with silane in order to immobilize HIV gp41 antibodies on their surfaces. The HIV pseudovirus was added to the treated substrates followed by addition of antibodies conjugated to nanoparticles. The surfaces were characterised by using water contact angle, atomic force microscopy (AFM) and Raman spectroscopy. Our preliminary data displayed that the antibodies were indeed immobilized on the glass substrates which made it possible for capturing the intact HIV pseudovirus. Further, Raman spectroscopy revealed the presence of disulphide bonds indicating successful conjugation of the HIV gp41 antibodies to the HIV pseudovirus.
COA
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Publication ()
Figure 1. HIV-1 viral entry
