NK cells from tuberculous pleurisy express high ICAM-1 levels and exert stimulatory effect on local T cells

Eur J Immunol. 2009 Sep;39(9):2450-8. doi: 10.1002/eji.200939515.

Abstract

Tuberculous pleurisy, one of the most common manifestations of extrapulmonary tuberculosis, is characterized by a T-cell-mediated hypersensitivity reaction along with a Th1 immune profile. In this study, we investigated functional cross-talk among T and NK cells in human tuberculous pleurisy. We found that endogenously activated pleural fluid-derived NK cells express high ICAM-1 levels and induce T-cell activation ex vivo through ICAM-1. Besides, upon in vitro stimulation with monokines and PAMP, resting peripheral blood NK cells increased ICAM-1 expression leading to cellular activation and Th1 polarization of autologous T cells. Furthermore, these effects were abolished by anti-ICAM-1 Ab. Hence, NK cells may contribute to the adaptive immune response by a direct cell-contact-dependent mechanism in the context of Mycobacterium tuberculosis infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • CD11a Antigen / immunology
  • CD56 Antigen / immunology
  • Cell Communication / immunology
  • Cysteine / analogs & derivatives
  • Cysteine / pharmacology
  • Humans
  • Intercellular Adhesion Molecule-1 / drug effects
  • Intercellular Adhesion Molecule-1 / immunology
  • Intercellular Adhesion Molecule-1 / metabolism*
  • Interleukin-12 / pharmacology
  • Interleukin-15 / pharmacology
  • Interleukin-18 / pharmacology
  • Killer Cells, Natural / immunology*
  • Lipopolysaccharides / pharmacology
  • Lipoproteins / pharmacology
  • Middle Aged
  • Mycobacterium tuberculosis*
  • Phosphotransferases (Phosphate Group Acceptor)
  • T-Lymphocytes / immunology*
  • Tuberculosis, Pleural / immunology*

Substances

  • CD11a Antigen
  • CD56 Antigen
  • Interleukin-15
  • Interleukin-18
  • Lipopolysaccharides
  • Lipoproteins
  • Intercellular Adhesion Molecule-1
  • Interleukin-12
  • 2,3-bis(palmitoyloxy)-2-propyl-1-palmitoylcysteine
  • Phosphotransferases (Phosphate Group Acceptor)
  • polyphosphate AMP phosphotransferase
  • Cysteine