Antibody studies into the human immunodeficiency virus (HIV) centre around Gag, a highly complex polyprotein that has so far defied attempts to unravel its complex and varied modes of action. Now, a team from the NIST Center for Neutron Research have revealed a new model which has allowed the protein to be studied in far more clarity. The hope with antibody suppliers is that it will pave the way to understanding many more large, unfathomable proteins.
HIV1 antibodies have uncovered at least some of the complexities of the Gag protein, which performs highly complex tasks during viral assembly, twisting into convoluted shapes within the host cell. During the initial stages, membrane associations are formed which enable HIV genetic material to be transported to the cell membrane. The opposite end of the Gag protein becomes anchored here, elongating into a rod-like shape which helps form a barrier around the virion particles. This leads to budding, maturation and dispersal. During viral assembly, Gag precursors selectively bind to and package genomic RNA strands. Many other proteins re involved – for example, Capsid protein p24, which is thought to form the core of the virus when encapsulation of the genomic RNA-nucleocapsid complex takes place.
However, while antibody studies have helped shed light on the multiple roles Gag plays in HIV assembly, the finer details have remained a mystery. Now, the NCNR team have developed an artificial cell membrane that enables viewing of Gag function with neutron probes. By mimicking various stages of viral development, the team were able to observe changes in Gag conformation – many of them never seen before.
We at Novus Biologicals carry a large number of antibodies for HIV research, a complex but fascinating area.
Novus Biologicals offers many HIV reagents for your research needs including:
