The survival of patients with HIV has been successfully prolonged due to antiretroviral therapy. However, the blood brain barrier (BBB) decreases the permeability of many drugs into the central nervous system. As a result, the brain can become infected, leading to neurocognitive disorders such as HIV associated dementia. Previous research showed that radioimmunotherapy (RIT) targeting the HIV gp41 glycoprotein successfully kills infected HIV cells and virions, eliminating HIV in tissue culture cells and in mice. Here we examined the ability of 2556, a gp41-specific radiolabeled monoclonal antibody, to take up the ligand CHXA� (trans-cyclohexyldiethylenetriamine) at different molar ratios, and tested to see if 2556-CHXA� was able to maintain its immunoreactivity to gp41, using a direct ELISA. We were successful in chelating 2556 to the ligand CHXA�. A starting molar excess of 50X CHXA� yielded 6X final molar excess of CHXA� attached to 2556, which retained about 30% of its original immunoreactivity. A starting molar excess of 2X yielded a final molar excess of 1X and 100% of the original immunoreactivity. We concluded that the lower the ratio of CHXA� to 2556 the more immunoreactivity the antibody retains. Ultimately, we will radiolabel the 2556-CHXA� complex with Bismuth to see how well the protein retains immunoreactivity, and we will examine 2556 and see if the protein's isoelectric point has been altered thus enabling it to easily enter through the BBB.Acknowledgements:Summer Undergraduate Research Program at Albert Einstein College of MedicineBill and Melinda Gates Foundation GCE GrantSpecial mention to Dina Tsukrov, Alicia McFarren, and Ekaterina Revskaya

Modification of antibody 2556 recognizing HIV protein gp41 with CHXA� ligand for radiolabeling and radioimmunotherapy

247th National Meeting (2014)

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