Recombinant HIV-2 gp32

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.

HIV-2 gp32 recombinant- contains the full-length sequence of HIV-2 envelope immunodominant regions gp32. The protein is fused with b-galactosidase (114 kDa) at N-terminus.

Escherichia Coli.

Sterile filtered colorless clear solution.

The HIV-2 gp32 solution (1mg/ml) 0.01M Na₂CO₃, 0.01M Na₃EDTA, 0.014 Mb-mercaptoethanol and 0.02% Sarcosyl.

Greater than 95.0% as determined by SDS-PAGE.

Protein should be stored at 4°C.
Refrigerate Upon arrival. DO NOT FREEZE.

Immunoreactive with all sera of HIV-2 infected individuals.

HIV-2 gp32 antigen is suitable for ELISA and Western blots, excellent antigen for early detection of HIV seroconvertors with minimal specificity problems.

SDS

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