The respiratory burst oxidase of phagocytes and B lymphocytes is a complicated enzyme that catalyzes the one-electron reduction of oxygen by NADPH. It is responsible for the O2/- production that occurs when these cells are exposed to phorbol 12-myristate 13-acetate or other appropriate stimuli. The activity of this enzyme is greatly decreased or absent in patients with chronic granulomatous disease, an inherited disorder characterized by a severe defect in host defense against bacteria and fungi. In every chronic granulomatous disease patient studied to date, an abnormality has been found in a gene encoding one of four components of the respiratory burst oxidase: the membrane protein p22(phox) or gp91(phox), or the cytosolic protein p47(phox) or p67(phox). We report here that O2/- production was partly restored to phorbol 12-myristate 13-acetate-stimulated Epstein-Barr virus-transformed B lymphocytes from a patient with p47(phox)- deficient chronic granulomatous disease by transfection with an expression plasmid containing a p47(phox) cDNA inserted in the sense direction. No detectable O2/- was produced by untransfected p47(phox)-deficient lymphocytes or by p47(phox)-deficient lymphocytes transfected with an antisense plasmid. The finding that O2/- can be produced by p47(phox)- deficient B lymphocytes after the transfer of a p47(phox) cDNA into the deficient cells suggests that this system could be useful for studying the function of mutant p47(phox) proteins in whole cells.
|Original language||English (US)|
|Number of pages||4|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - 1992|
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