HIV-2 is a type of Human Immunodeficiency Virus (HIV) that is less prevalent and generally less pathogenic than HIV-1. The envelope glycoproteins of HIV-2 play a crucial role in the virus’s ability to infect host cells. One of these glycoproteins is gp36, which is a transmembrane protein involved in the fusion of the virus with the host cell membrane.
The HIV-2 envelope is composed of two main glycoproteins: gp125 and gp36. These proteins are linked by noncovalent bonds and are embedded in a lipid bilayer derived from the host cell’s cytoplasmic membrane . The gp125 protein is responsible for binding to the host cell receptors, while gp36 mediates the fusion of the viral and host cell membranes .
Gp36 is a 36 kDa protein that is produced as part of a larger polyprotein precursor. This precursor undergoes glycosylation in the Golgi apparatus and is then cleaved by furin in the trans-Golgi network to produce the mature gp36 protein . The cleavage positions the fusion peptide at the N-terminus of gp36, priming it for fusion activation .
Synthetic HIV-2 gp36 refers to the recombinant form of the gp36 protein, which is produced using various biotechnological methods. This synthetic form is often used in research and diagnostic applications. For instance, synthetic gp36 can be produced in Escherichia coli and is often fused to other proteins, such as beta-galactosidase, to facilitate its purification and detection .
The synthetic gp36 protein retains the immunodominant regions of the natural protein, making it useful for studying the immune response to HIV-2 and for developing diagnostic assays . It is also used in the development of vaccines and therapeutic agents aimed at preventing or treating HIV-2 infection .
The study of synthetic HIV-2 gp36 is important for several reasons: