Compositions for promoting HIV-1 virolysis and methods using same

PAGE TITLE

Compounds for promoting HIV-1 virolysis

 

PAGE SUMMARY

Globally, there are about 37 million people living with HIV/AIDS and 1.2 million died from AIDS-related illnesses in 2014.  In the US, over 1.1 million live with HIV/AIDS and 50,000 new cases are reported each year.  The HIV therapeutics market was valued at $14.3 billion in 2012 and is expected to reach $16.3 billion by 2019.  While highly active anti-retroviral therapy (HAART) delays the onset of AIDS, it does not provide a cure for HIV infection.  Similarly, there are no clinically used agents that directly destroy mature HIV-1 virions before the particles enter the host cell.

 

Researchers in the Chaiken lab have created a fusion protein with specific HIV-1 antiviral activity that simultaneously binds to both virus Env protein subunits.  More specifically, the fusion is the lectin cyanovirin-N (CVN) and the gp41 membrane-proximal external region peptide (MPER).  Engaging these viral proteins destabilizes viral entry, inactivating the virus before it can enter the host cell.  While there are a few examples in the literature of two-component fusions as HIV-1 inhibitors, this work is the first example that specifically achieves highly potent lytic inactivation of HIV-1.  Testing is planned to measure the effects on Env-expressing cells.

 

APPLICATIONS

TITLE: Applications

 

HIV-1 cell-free virolysis

Prevent HIV-1 infection by inactivating virus at early stage of exposure, prior to host cell encounter

Target and irreversibly destroy mature HIV-1 particles

 

ADVANTAGES

TITLE:Advantages

 

Simultaneously target different stages of viral life cycle

Reduce evolutionary adaptability and drug resistance of HIV

Nontoxic to host cells

 

IP STATUS

Intellectual Property and Development Status

Issued United States Patent 9,233,138

https://patents.google.com/patent/US9233138B2/en

 

PUBLICATIONS

References

 

Parajuli, B. et al. Lytic inactivation of HIV-1 by Dual Engagement of gp120 and gp41 Domains in the Virus Env Protein Trimer.  Biochemistry, 2016, 55(44): p. 6100-6114.

http://pubs.acs.org/doi/abs/10.1021/acs.biochem.6b00570

 

Contarino M. et al.  Chimeric cyanovirin-MPER recombinantly engineered proteins cause cell-free virolysis of HIV-1.  Antimicrobial Agents and Chemotherapy, 2013, 57(10), p. 4743-4750.

http://aac.asm.org/content/57/10/4743.full

 

Drexel News.

http://drexel.edu/now/archive/2013/september/davei-hiv-molecule/

 

Contact Information     

Tanvi Muni, PhD

Licensing Manager,

Drexel Applied Innovation

Office of Research and Innovation

3250 Chestnut Street, Ste. 3010
Philadelphia, PA 19104

Phone:267-359-5640

Email:tanvi.muni@drexel.edu

 

Patent Information: