AIDSWEEKLY Plus; Monday, August 10 & 17, 1998
Daniel J. DeNoon, Senior Editor
The AIDS virus docks to susceptible cells via specific chemokine receptors. Since chemokines act as cellular messengers that tell T cells when and where to go, it is possible that HIV binding itself sends a message affecting T-cell trafficking.
Claudia Cicala and colleagues at Anthony Fauci's National Institutes of Health laboratory discovered that this is exactly the case.
"HIV may recruit uninfected target cells to areas with high concentration of virus such as lymphoid tissue," Cicala said in a presentation to the 12th World AIDS Conference, held June 28-July 3, 1998, in Geneva, Switzerland.
The NIH research team performed an elaborate series of experiments to identify signals resulting from HIV binding to the CCR5 (R5) chemokine receptor. They found that the HIV Env protein initiated several phosphorylation events.
One of these events involves the focal adhesion kinase (FAK) receptor. FAK forms the focal adhesion complex that mediates signal transduction processes. It is involved in at least three signalling pathways.
Cicala and colleagues found that Env treatment of CD4(+) T cells led to redistribution of FAK complexes and induced co-localization of R5 and FAK.
"Identification of this novel HIV mediated intracellular signalling pathway suggests a mechanism by which HIV envelope can dysregulate trafficking of CD4(+) T cells," she said.
When asked whether she had any in vivo evidence of FAK activation interfering with in T-cell homing mechanisms, Cicala noted that only one patient had been tested. She said that FAK dysregulation in this patient, who rapidly progressed to AIDS after HIV infection, "was quite striking."
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