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Archive - Aug 22, 2015

“Molecular Tweezer” (CLR01) Shows Remarkable Potential Effectiveness Against HIV and Other Sexually Transmitted Viruses in Semen

An unprecedented potential "molecular tweezer" called CLR01, reported on August 18, 2015 in the open-access journal eLife, not only blocks HIV and other sexually transmitted viruses, but also breaks up proteins in semen that boost infection. The article is titled “'A Molecular Tweezer Antagonizes Seminal amyloids and HIV Infection.” Semen is the main vector for sexual HIV transmission. It contains proteins that assemble into very stable polymers called amyloid fibrils, which can enhance HIV infectivity by up to 10,000 times. Scientists, led by the University of Pennsylvania (USA) and the University of Ulm (Germany), now show that a molecule with the shape of a tweezer not only destroys HIV particles, but also blocks the infection-promoting activity of semen amyloids. The antiviral activity of CLR01 is based on the way it selectively interacts with and destroys the viral coat. Remarkably, CLR01 does not affect cell membranes, which suggests it could be safely incorporated into a vaginal or anal gel to prevent HIV infection - without the risk of side effects. The way CLR01 operates means that it is also effective against many other sexually transmitted viruses, including hepatitis C and viruses in the herpes family. It may also be effective against many other "enveloped" viruses including flu and Ebola. The use of other preventive treatments has been undermined in some countries by the stigma associated with HIV. As CLR01 is effective against many viruses besides HIV, it could be more widely acceptable as a general protective agent in communities struggling with HIV stigma. Moreover, the scientists found that CLR01 also binds to amyloid fibrils and prevents the interaction with viruses that could be exploited by HIV to boost sexual transmission.

New Data on Mechanism of Cilia Assembly; Pertinent to Polycystic Kideny Disease (PKD) and Other Ciliopathies

The group led by ICREA (Catalan Institution for Research and Advanced Studies) Research Professor Cayetano Gonzalez at IRB Institute for Research in BiomedicineBarcelona, in collaboration with the group of Professor Giuliano Callaini from the University of Siena in Italy, has published a new study online on August 20, 2015 in Current Biology that contributes to understanding how cilia are assembled. The article is titled “Loss of Centrobin Enables Daughter Centrioles to Form Sensory Cilia in Drosophila.” Many cells in human bodies present a small structure that looks like, and as a matter of fact works as an antenna, conveying to the cell information on the extracellular environment. These structures are called cilia (plural) or cilium (singular). Ciliated cells play essential functions in the human body. Thus, for instance, the monitoring of fluid flow in the kidney, the detection of hormones in the brain, or the senses of hearing and smell depend on specialized neurons equipped with chemo-sensory or mechano-sensory cilia. Moreover, besides a sensory role, beating cilia keep fluids in motion in many parts of our bodies and are critical for human health. A cilium can be regarded as a long and thin protrusion of the cell membrane that contains microtubules. Ciliary microtubules are arranged in a typical radial symmetry that is conserved through evolution and is templated by a small organelle that sits at the base of the cilium, known as a basal body. Most animal cells contain two basal body-like structures (centrioles), but only one of them can actually work as basal body. In human cells, this is always the centriole that is said to be the "mother" because it was assembled earlier than the other, called the "daughter" centriole.