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Mutation Breaks HIV’s Resistance to Drugs, Says MU Researcher

Doctors can improve treatment programs using this knowledge

COLUMBIA, Mo. – The human immunodeficiency virus (HIV) can contain dozens of different mutations, called polymorphisms. In a recent study an international team of researchers, including University of Missouri scientists, found that one of those mutations, called 172K, made certain forms of the virus more susceptible to treatment. Soon, doctors will be able to use this knowledge to improve the drug regimen they prescribe to HIV-infected individuals.

“The 172K polymorphism makes certain forms of HIV less resistant to drugs,” said Stefan Sarafianos, corresponding author of the study and a researcher at MU’s Bond Life Sciences Center. “172K doesn’t affect the virus’ normal activities. In some varieties of HIV that have developed resistance to drugs, when the 172K mutation is present, resistance to two classes of anti-HIV drugs is suppressed. We estimate up to 3 percent of HIV strains carry the 172K polymorphism.” (more…)

Clearing a Potential Road Block to Bisabolane

By Guest PostJanuary 14, 2012Scienceabies grandis, abies grandis α bisabolene synthase, advanced biofuels, agbis, andy degiovanni, berkeley lab, biofuel, biosynthetic alternative, bisabolane, ca, chemical compounds, cofactors, d2 diesel fuel, emeryville, enzyme, evolutionary heritage, flavorings, fragrances, grand fir, green energy, inhibitors, jay keasling, jose pereira, masood hadi, microbes, microbial based production, pamela peralta yahya, paul adams, precursor, protein, protein crystal structure, renewable alternative, resolution, ryan mcandrew, synthases in plants, terpene class, terpenoid synthases, three dimensional crystal structure, trucking industry, united states, x ray crystallography

*Joint BioEnergy Institute Researchers Identify Key Enzyme Structure*

The recent discovery that bisabolane, a member of the terpene class of chemical compounds used in fragrances and flavorings, holds high promise as a biosynthetic alternative to D2 diesel fuel has generated keen interest in the green energy community and the trucking industry. Now a second team of researchers with the U.S Department of Energy (DOE)’s Joint BioEnergy Institute (JBEI) has determined the three-dimensional crystal structure of a protein that is key to boosting the microbial-based production of bisabolane as an advanced biofuel.

The JBEI research team, led by bioengineers Paul Adams and Jay Keasling, solved the protein crystal structure of an enzyme in the Grand fir (Abies grandis) that synthesizes bisabolene, the immediate terpene precursor to bisabolane. The performance of this enzyme – the Abies grandis α-bisabolene synthase (AgBIS) – when engineered into microbes, has resulted in a bottleneck that hampers the conversion by the microbes of simple sugars into bisabolene. (more…)

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Mutation Breaks HIV’s Resistance to Drugs, Says MU Researcher

Clearing a Potential Road Block to Bisabolane