Cellular armature against HIV
Date: 18.8.2010
A team of researchers at the University of the Basque Countries, the Autonomous University of Madrid and the Institute of Applied Chemistry of Catalonia in Barcelona studied a possibility how to block the enter of the HIV into the cell by changing the level of the cell membrane fluidity. The researchers published their results in an article in the journal Chemistry & Biology (Vieira et al., 2010).
Almost all currently available treatments against HIV are based on attempts to block the replication of the virus once it has penetrated the cell. "In fact there is only one product, which is able to prevent the inoculation of the viral material in the cell. It is enfurvitide, but this drug is based on a principle completely different from that used in our research, " says Felix Goñi, who directed the study.
The new working hypothesis is based on adjusting the fluidity of cell membranes to avoid the fusion process between the cell membrane and the virus, which represents a key step in the infection.
"After the cell membranes and the virus come into contact with each other, a "hole" opens and the virus can enter. The membranes must have a degree of fluidity and mobility. We have discovered a procedure that makes the cell membranes more rigid. This could give rise to a new type of drugs that stop the virus from entering by increasing the rigidity of the membrane. We are going to produce a kind of an armature that makes the cell impenetrable, " says Goñi.
Researchers have synthesized a molecule that blocks an enzyme, dihydroceramide desaturase, which prevents the transformation of the normal sphingolipids in the cell membrane into dihydrosfingolipids. These ones make the membrane rigid enough to prevent entry of the virus.
References:
Story source: http://lescienze.espresso.repubblica.it/ translated by Pavla Čermáková
Original work: Catarina R. Vieira, Jose M. Munoz-Olaya, Jesús Sot, Sonia Jiménez-Baranda, et al. (2010): Dihydrosphingomyelin Impairs HIV-1 Infection by Rigidifying Liquid-Ordered Membrane Domains. Chemistry & Biology; 17 (7):
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