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Cysteine Proteases ofTrichomonas vaginalisDegrade Secretory Leukocyte Protease Inhibitor
Author(s) -
Deborah Draper,
William Donohoe,
Leo F. Mortimer,
R. Phillip Heine
Publication year - 1998
Publication title -
the journal of infectious diseases
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/515366
Subject(s) - slpi , proteases , trichomonas vaginalis , biology , saliva , microbiology and biotechnology , cysteine protease , trichomoniasis , virology , protease inhibitor (pharmacology) , immunology , virus , enzyme , medicine , biochemistry , inflammation , antiretroviral therapy , viral load , pathology
Sexually transmitted diseases, including trichomoniasis, are risk factors for acquisition of human immunodeficiency virus (HIV) infection. Enhancement mechanisms are unknown. Secretory leukocyte protease inhibitor (SLPI) from saliva appears to prevent transmission of HIV through inhibition of virus entry into monocytic cells in vitro. This study was undertaken to determine if secreted cysteine proteases of Trichomonas vaginalis degrade SLPI and render it nonfunctional. It was determined if SLPI levels were decreased in vaginal fluids from pregnant women infected with T. vaginalis. Isolated proteases were incubated with recombinant human SLPI, and the degradation was followed by Western analysis with SLPI antiserum. SLPI levels were measured by ELISA in vaginal fluids from women infected with T. vaginalis and uninfected controls. Cysteine proteases cleaved SLPI and rendered it nonfunctional. Median levels of SLPI from infected patients were 26% of those of controls (P <.005). The degradation of SLPI in association with trichomonal infection may increase the risk of HIV acquisition.

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