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Lethal oxidative damage to human immunodeficiency virus by human recombinant myeloperoxidase
Author(s) -
Moguilevsky Nicole,
Steens Martine,
Thiriart Clotilde,
Prieels Jean-Paul,
Thiry Lise,
Bollen Alex
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80442-j
Subject(s) - recombinant dna , myeloperoxidase , intracellular , virology , viral replication , virus , biology , chemistry , microbiology and biotechnology , biochemistry , immunology , gene , inflammation
Human recombinant myeloperoxidase was evaluated in a cell‐free system for its inactivation properties on the replication of human immunodeficiency virus, HTLV‐III B . In the presence of a hydrogen peroxide generating system (glucose and glucose oxidase) and sodium thiocyanate, the recombinant enzyme inhibited virus‐induced syncytium formation and viral replication without causing any cytopathic effects on SupT1 reporter cells. In addition, U937 monocytoid cells, chronically infected with HIV1, were exposed to recombinant myeloperoxidase (10 U/ml) and monitored during 48 h for the accumulation of intracellular p24 viral antigen. Under these conditions, the recombinant enzyme significantly reduced intracellular viral replication without affecting cell viability.