Virucidal effect of myeloperoxidase on human immunodeficiency virus type 1-infected T cells

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Published inAntimicrobial Agents and Chemotherapy Vol. 38; no. 5; pp. 969 - 972
Main Authors CHOCHOLA, J, YAMAGUCHI, Y, MOGUILEVSKY, N, BOLLEN, A, STROSBERG, A. D, STANISLAWSKI, M
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.05.1994
Subjects
AIDS/HIV
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antiviral Agents
Antiviral Agents - pharmacology
Biological and medical sciences
Catalase - pharmacology
Cell Line
Glucose Oxidase - pharmacology
HIV Core Protein p24 - immunology
HIV Core Protein p24 - metabolism
HIV-1
HIV-1 - drug effects
HIV-1 - metabolism
human immunodeficiency virus 1
Humans
Lactoperoxidase - pharmacology
Medical sciences
Peroxidase
Peroxidase - pharmacology
Pharmacology. Drug treatments
Phytohemagglutinins - pharmacology
Radioimmunoassay
Research Article
T-Lymphocytes
T-Lymphocytes - drug effects
T-Lymphocytes - microbiology
Cell culture
HIV-1 virus
Enzyme
Retroviridae
Cytotoxicity
In vitro
Virus
Cell line
Sensitivity resistance
T-Lymphocyte
Lentivirinae
Antiviral
Human immunodeficiency virus
Infected cell
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AbstractList Myeloperoxidase is virucidal to human immunodeficiency virus type 1 (HIV-1) in the persistently infected CEM human T-cell line or in acutely infected human peripheral blood mononuclear cells, as judged by viral infectivity and P24 radioimmunoassay. HIV-1 was specifically inactivated by low doses of the human myeloperoxidase (1.4 to 14.3 mU/ml) and the cells were spared. A higher enzyme concentration (143 mU/m) was cytotoxic, but uninfected CEM cells and normal lymphocytes were resistant to > or = 143 mU of myeloperoxidase per ml. The enzyme was virucidal with the Cl- present in medium and did not require exogenous H2O2. Catalase, an antioxidant enzyme, partially inhibited the virucidal effect of myeloperoxidase. Hence, the H2O2 probably came from the HIV-infected cells themselves. These in vitro findings indicate that the myeloperoxidase system is capable of inactivating HIV-1 of infected cells.
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Myeloperoxidase is virucidal to human immunodeficiency virus type 1 (HIV-1) in the persistently infected CEM human T-cell line or in acutely infected human peripheral blood mononuclear cells, as judged by viral infectivity and P24 radioimmunoassay. HIV-1 was specifically inactivated by low doses of the human myeloperoxidase (1.4 to 14.3 mU/ml) and the cells were spared. A higher enzyme concentration (143 mU/m) was cytotoxic, but uninfected CEM cells and normal lymphocytes were resistant to greater than or equal to 143 mU of myeloperoxidase per ml. The enzyme was virucidal with the Cl super(-) present in medium and did not require exogenous H sub(2)O sub(2). Catalase, an antioxidant enzyme, partially inhibited the virucidal effect of myeloperoxidase. Hence, the H sub(2)O sub(2) probably came from the HIV-infected cells themselves. These in vitro findings indicate that the myeloperoxidase system is capable of inactivating HIV-1 of infected cells.
Author A D Strosberg
J Chochola
N Moguilevsky
Y Yamaguchi
M Stanislawski
A Bollen
AuthorAffiliation Laboratoire d'Immunologie, Institut de Recherches Scientifiques sur le Cancer, Villejuif, France
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Keywords Cell culture
HIV-1 virus
Enzyme
Retroviridae
Cytotoxicity
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Cell line
Sensitivity resistance
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Lentivirinae
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Human immunodeficiency virus
Infected cell
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SubjectTerms AIDS/HIV
Antibiotics. Antiinfectious agents. Antiparasitic agents
Antiviral Agents
Antiviral Agents - pharmacology
Biological and medical sciences
Catalase - pharmacology
Cell Line
Glucose Oxidase - pharmacology
HIV Core Protein p24 - immunology
HIV Core Protein p24 - metabolism
HIV-1
HIV-1 - drug effects
HIV-1 - metabolism
human immunodeficiency virus 1
Humans
Lactoperoxidase - pharmacology
Medical sciences
Peroxidase
Peroxidase - pharmacology
Pharmacology. Drug treatments
Phytohemagglutinins - pharmacology
Radioimmunoassay
Research Article
T-Lymphocytes
T-Lymphocytes - drug effects
T-Lymphocytes - microbiology
Title Virucidal effect of myeloperoxidase on human immunodeficiency virus type 1-infected T cells
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