ORGANIZATION OF FOCAL ADHESION PLAQUES IS DISRUPTED BY ACTION OF THE HIV‐1 PROTEASE

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Abstract
Focal adhesion plaques were severely affected in human embryonic fibroblasts permeabilized with digitonin and incubated in buffer containing the human immunodeficiency virus type 1 protease (HIV−1 PR). A mutant HIV−1 PR (3271 HIV−1 PR) had no effect on focal adhesion plaques. Similar effects were seen with cells microinjected with either HIV−1 PR or 3271 HIV−1 PR. Immunoblots of the human embryonic fibroblasts demonstrated that a number of focal adhesion plaque proteins were specifically cleaved by HIV−1 PR. These included fimbrin, focal adhesion plaque kinase (FAK), talin, and, to a lesser extent, filamin, spectrin and fibronectin. Proteins detected by antibodies to 4 integrin and 3 integrin were also cleaved by the HIV−1 PR. Control experiments demonstrated that the effect and protein cleavages described are due to action of the HIV−1 PR and not to the action of endogenous host cell protease

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