Skip to main content

Thank you for visiting You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.


Gag helps make HIV buds

The researchers (clockwise from left) Jayanta Bhattacharya, Ajit Patil and Archana Gautam.

Highly active antiretroviral therapy (HAART) to immobilize key HIV enzymes such as reverse transcriptase and protease has improved the condition of many HIV infected. However, with the advent of drug resistant HIV variants, it has become imperative to identify alternate targets.

New research1 seeking to unravel the mechanism by which the envelope protein of HIV-1 assembles into infectious virus particles, has provided some answers. Researchers say the 'Gag' protein of HIV-1 by acting as cargo transport intermediate, carries the envelope protein and assembles them into budding virions that act as the infectious agents.

The Gag protein takes the trans-golgi route sorting into domains of lipid rafts enabling the assembly of the virions in primary CD4+ T cells. Lipid rafts are small groups of lipids and cholesterol on the cell surface of the infected primary CD4+ T cells that are natural targets of HIV-1 in vivo.

"We envisage that compounds that would interfere in the gag-envelope interaction will lead to the abolition of HIV-1 envelope assembly into budding virus particles. This will lead to production of defective infectious virus particles and limit virus entry," says lead researcher Jayanta Bhattacharya.



  1. Patil, A. et al. Evidence that Gag facilitates HIV-1 envelope association both in GPI-enriched plasma membrane and detergent resistant membranes and facilitates envelope incorporation onto virions in primary CD4+ T cells. Virol. J. 7 (2010) doi: 10.1186/1743-422X-7-3

    PubMed  Google Scholar 

Download references

Nature Careers


Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing


Quick links