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Related Experiment Videos

Cryptococcal polysaccharides bind to CD18 on human neutrophils

Z M Dong1, J W Murphy

  • 1Department of Microbiology and Immunology, University of Oklahoma Health Science Center, Oklahoma City 73190, USA.

Infection and Immunity
|February 1, 1997
PubMed
Summary

Cryptococcal culture filtrate (CneF) and its components, glucuronoxylomannan (GXM) and galactoxylomannan (GalXM), bind to CD18 on neutrophils. This interaction may inhibit leukocyte infiltration into inflammatory sites.

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Area of Science:

  • Immunology
  • Microbiology
  • Cell Biology

Background:

  • CD18 is a key adhesion molecule on leukocytes, crucial for neutrophil migration to inflammatory sites.
  • Cryptococcal culture filtrate (CneF) has been shown to inhibit neutrophil accumulation.
  • Understanding CneF's mechanism of action is vital for managing cryptococcosis.

Purpose of the Study:

  • To investigate the interaction between CneF and its components with CD18 on human neutrophils.
  • To determine if CD18 is a molecular target for cryptococcal polysaccharides.

Main Methods:

  • Human neutrophils were incubated with 14C-labeled CneF.
  • Monoclonal antibodies against CD18 and CD11a were used to block binding.
  • Indirect immunofluorescence staining and flow cytometry analyzed the binding of CneF, GXM, GalXM, and MP to neutrophils.

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Main Results:

  • 14C-labeled CneF bound to human neutrophils in a dose-dependent manner.
  • Anti-CD18 antibodies blocked CneF binding, indicating CD18 as the binding site.
  • CneF, GXM, and GalXM inhibited anti-CD18 antibody binding, suggesting they interact with CD18.

Conclusions:

  • Cryptococcal components, specifically GXM and GalXM, bind to CD18 on human neutrophils.
  • CD18 is a potential molecular target for cryptococcal polysaccharides.
  • This binding may underlie the inhibition of leukocyte infiltration observed in cryptococcosis.