Please read on. The article goes on conclude

"After eliminating the weaker and more toxic candidates with further tests, Breuer, Torbett, and their colleagues ended up with 10 compounds. Detailed analyses of these yielded two that were sufficiently powerful at inhibiting viral infectivity in cell culture tests, without being unacceptably toxic.

"We went very quickly from having a concept to having these two inhibitors with demonstrated anti-HIV activity in cells," said Torbett.

Searching for the 'Sweet Spot'

With his Scripps Research colleagues M. G. Finn and Valery Fokin, Torbett now plans to evaluate compounds that are closely related to the two inhibitors to see if the scientists can find any that are even more safe and effective. Torbett and colleagues also plan to apply the same combination-screening method to larger compound libraries to identify entirely new nucleocapsid-inhibiting compounds.

To gain a better understanding of how these inhibitors work, Torbett is also collaborating with Scripps Research structural biologists, including David Stout and Arthur Olson, and virologist John Elder to perform X-ray crystallography studies of the inhibitors in combination with the HIV nucleocapsid protein.

"The overall goal here is to find a 'sweet spot' on the nucleocapsid protein that can be targeted effectively by a small-molecule drug without causing toxicity," Torbett said."

Perhaps even we in the World Community Grid may be asked to assist in this research at some future point in time.

More than 20,000 international HIV researchers and activists will gather in the nation's capital later this month with a sense of optimism not seen in many years, hope that it finally may be possible to dramatically stem the spread of the AIDS virus.

http://www.wtop.com/267/2934265/New-optimism-about-curbing-AIDS

http://www.sciencecodex.com/uw_scientists_dis...fight_hiv_infection-94855

[...] the viral protein vpu, which is created by HIV during infection, directly interferes with the immune response protein IRF3 to dampen the ability of the immune system to protect against virus infection. [...] the HIV protein vpu specifically binds to the immune protein IRF3 and targets it for destruction, thereby, preventing IRF3 from functioning to trigger an immune response within the infected cell. [...] HIV strains engineered to lack vpu, which is made during infection, did not impair the immune response.

"We have effectively identified a new Achilles heel in the arsenal that HIV uses to overcome the defenses present in the body's immune system", stated Dr. Gale. "This knowledge can be used to design new HIV antiviral therapeutics that prevent vpu from interacting with IRF3 and targeting it for destruction, thus enhancing immunity. [...]

http://www.sciencedaily.com/releases/2012/07/120717141233.htm

ScienceDaily (July 17, 2012) — A new collection of compounds, called "bryologs" -- derived from a tiny marine organism -- activate hidden reservoirs of the virus that currently make [AIDS] nearly impossible to eradicate. [...] The first attempts to reactivate latent HIV were inspired by observations of Samoan healers. When ethnobotanists examined the bark of Samoa's mamala tree, traditionally used by healers to treat hepatitis, they found a compound known as prostratin. Prostratin binds to and activates protein kinase C, an enzyme that forms part of the signaling pathway that reactivates latent viruses. The discovery sparked interest in the enzyme as a potential therapeutic target, especially as it was discovered that prostratin isn't the only biomolecule to bind to the kinase. The bryozoan Bugula neritina - a mossy, colonial marine organism -- produces a protein kinase C-activating compound that is many times more potent than prostratin. The molecule, named bryostatin 1, was deemed to hold promise as a treatment, not only for HIV but for cancer and Alzheimer's disease as well. [...] Wender, who published the first practical synthesis of prostratin and its analogs in 2008, had set out to make a simpler, more effective synthetic analog of bryostatin. [...] The seven resulting compounds, called bryologs, share two fundamental features with the original bryostatin: the recognition domain, which directly contacts protein kinase C, and the spacer domain, which allows the bryolog-protein kinase C complex to be inserted into the cell membrane. The researchers tested the new compounds' ability to reactivate viral reservoirs in J-Lat cell lines, which contain latent HIV and begin to fluoresce when they express the virus. In the J-Lat line, bryologs induced virus in as many or more cells than bryostatin at a variety of concentrations, and ranged from 25 to 1,000 times more potent than prostratin. The compounds showed no toxic effects. Bryolog testing remains in the early stages -- the researchers are currently conducting in vivo studies in animal models. But practical bryostatin substitutes may be the first step toward true HIV-eradication therapy.

http://www.sciencedaily.com/releases/2012/07/120719132725.htm

Potent new compound virtually eliminates HIV in cell culture

A new study by scientists on the Florida campus of The Scripps Research Institute shows, in cell culture, a natural compound can virtually eliminate human immunodeficiency virus (HIV) in infected cells. The compound defines a novel class of HIV anti-viral drugs endowed with the capacity to repress viral replication in acutely and chronically infected cells. [...] "The compound in the current study virtually eliminates all viral replication from already-infected cells where HIV hides."

The new study, published in the July 20, 2012 issue of the journal Cell Host and Microbe, focused on a medically promising compound known as Cortistatin A. This natural product was isolated in 2006 from a marine sponge, Corticium simplex, discovered more than 100 years ago. In 2008, Scripps Research chemist Phil Baran and his team won the global race to synthesize the compound, presenting an efficient and economical method. In the new study, Valente and her colleagues collaborated with the Baran lab, using a synthetic version of the compound, didehydro-Cortistatin A, to study the compound's effect on two strains of HIV. The strains were HIV-1, the most common form of the virus, and HIV-2, which is concentrated in West Africa and some parts of Europe. [...]

The results showed that the compound reduced viral production by 99.7 percent from primary CD4+T cells (a type of immune cell) isolated from patients without levels of the virus in their bloodstream and who had been under HAART treatment for a long period of time. When the compound was added to other antiviral treatments, it further reduced by 20 percent viral replication from CD4+T cells isolated from patients with detectable amounts of virus in their bloodstreams. The inhibitor works by binding tightly to the viral protein known as Tat, a potent activator of HIV gene expression, effectively preventing the virus from replicating even at miniscule concentrations—making it the most potent anti-Tat inhibitor described to date, Valente said. Another interesting feature of this compound is that withdrawal of the drug from cell culture does not result in virus rebound, which is normally observed with other antiretrovirals. While most antiretroviral compounds block only new infections, didehydro-Cortistatin A reduces viral replication from already-infected cells, potentially limiting cell-to-cell transmission. The new inhibitor already has a drug-like structure, is effective at very low concentrations, and has no toxicity associated with it, at least at the cellular level, the study noted.