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Secretory leukocyte protease inhibitor inhibits infection of monocytes and lymphocytes with human immunodeficiency virus type 1 but does not interfere with transcytosis of cell-associated virus across tight epithelial barriers.

Abstract
In the present study, we demonstrate that recombinant human secretory leukocyte protease inhibitor (rhSLPI) inhibits infection of lymphocyte- and monocyte-derived tumor cell lines and peripheral blood lymphocytes with laboratory-adapted isolates and with the primary isolate, NDK, of free human immunodeficiency virus type 1 (HIV-1). In contrast, rhSLPI did not exhibit inhibitory activity toward transcytosis of cell-associated HIV-1 through a tight monolayer of endometrial epithelial cells. These observations indicate that the inhibitory effect of SLPI is restricted to free HIV-1 in corporal fluids.
AuthorsH Hocini, P Becquart, H Bouhlal, H Adle-Biassette, M D Kazatchkine, L Bélec
JournalClinical and diagnostic laboratory immunology (Clin Diagn Lab Immunol) Vol. 7 Issue 3 Pg. 515-8 (May 2000) ISSN: 1071-412X [Print] United States
PMID10799472 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins
  • RNA, Messenger
  • Recombinant Proteins
  • SLPI protein, human
  • Secretory Leukocyte Peptidase Inhibitor
  • Serine Proteinase Inhibitors
Topics
  • Acquired Immunodeficiency Syndrome (immunology, prevention & control, transmission)
  • Cervix Uteri (cytology, virology)
  • Epithelial Cells (drug effects, metabolism, virology)
  • Female
  • Gene Expression (immunology)
  • HIV Seronegativity
  • HIV-1
  • Humans
  • Lymphocytes (drug effects, metabolism, virology)
  • Monocytes (drug effects, metabolism, virology)
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins (genetics, immunology, pharmacology)
  • RNA, Messenger (analysis)
  • Recombinant Proteins (pharmacology)
  • Secretory Leukocyte Peptidase Inhibitor
  • Serine Proteinase Inhibitors (immunology, pharmacology)
  • Tight Junctions (metabolism, virology)

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