Adenovirus-dependent release of choline from plasma membrane vesicles at an acidic pH is mediated by the penton base protein.

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It has been suggested that during receptor-mediated endocytosis of human adenovirus (Ad) type 2 into cells, Ad disrupts the membrane of endocytic vesicles to enter the cytosol. To understand the mechanism of Ad-mediated disruption of the endocytic vesicles, I exposed Ad to plasma membrane vesicles derived from KB cells. Ad caused release of choline from the plasma membrane vesicles preloaded with [3H]choline. The efflux of choline was dependent on (i) the concentration of Ad, with a half-maximal effect at 0.5 microgram/ml; (ii) the pH of the buffer, with the optimum pH of the reaction ranging from 5.5 to 6.0; (iii) the length of the incubation, with a half-maximal release at 2 min; and (iv) the temperature of the incubation, with the optimum temperature being 37 degrees C. The Ad-dependent release of choline was inhibited by anti-penton base, while antihexon did not block the effect. These results suggest roles for a low-pH environment and the penton base protein in the Ad-dependent efflux of choline from plasma membrane vesicles.

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