Human immunodeficiency virus-1 (HIV-1) is a retrovirus, the most common form of HIV. HIV-1 attacks your body's immune system by destroying the CD4 cells that help your body fight infection, which can lead to acquired immunodeficiency syndrome (AIDS). The main structural proteins of HIV-1 are Gag and Gag/Pol, both precursor proteins encoded by viral genomic RNA. It has been shown that during HIV-1 replication, biomolecular condensates are involved in the entry and assembly phases of the viral replication cycle and that the main determinant of phase separation is the nucleocapsid domain of the Gag structural protein. Despite recent seminal observations, the importance of biomolecular condensates in HIV-1 has not been fully characterized. Therefore, it is important to address the fundamental question of the mechanisms by which HIV-1 forms biomolecular condensates and how these condensates contribute to efficient viral replicat.

Fig. 1. Viral replication cycles of HIV-1 and SARS-CoV-2 and implications of condensates generated by phase separation. (Wang B, et al., 2021)

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Many retroviral Gag structural domains have intrinsically disordered structural domains juxtaposed with RNA binding domains. In addition, HIV-1 Gag biomolecular condensates exhibit fluid-like behavior characterized by fluid motion, fusion, and fission. Our laboratory has successfully established a systematic virtual system for HIV-1 encoded proteins to analyze viral components with intrinsic disorders.

CD BioSciences provides professional services to analyze biomolecular condensates of intrinsically disordered HIV-1 nucleocapsid proteins assembled with viral genomic RNA by liquid-liquid phase separation (LLPS) to help clients obtain geometric characterization of viral retrotransposon complexes. We also focus on our exploration of the susceptibility, mechanism and pharmacological sensitivity of HIV-1Gag biomolecular condensates in living cells.

We offer a rigorous combination of biochemical and live cell imaging techniques to characterize the propensity for HIV-1 core protein phase separation in vitro and in live cells, including biomolecular condensates at early and late steps of the HIV-1 replication cycle

• HIV-1 early nuclear post-entry steps: we provide sophisticated real-time imaging methods to provide single-cell spatial information by tracking individual viruses, primarily phase separation of CPSF6.
• HIV-1 late nuclear post-entry steps: we provide HIV-1 ANCHOR system to label newly synthesized double-stranded viral DNA, and analyze viral DNA nucleodynamics to provide information on the evolution of HIV infection.
  

Importantly, our technical team is developing recombinant vaccines based on the HIV-1 nucleocapsid protein for antiviral immunity, and investigating antiviral strategies that allow the HIV-1 nucleocapsid protein to be used as a potential drug target.

Combining microscopy, biochemical and biophysical techniques, we offer a multifaceted approach to analyze LLPS in HIV-1 infection. CD BioSciences aims to help clients analyze the formation, kinetics and function of LLPS in viral assembly and maturation to develop potential therapeutic strategies for HIV-1. Our services are widely used in preclinical research on HIV-1 infection biology, diagnosis and treatment. If you are interested in our services, please feel free to contact us.