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Related Experiment Videos

The mast cell function-associated antigen exhibits saccharide binding capacity

R Binsack1, I Pecht

  • 1Department of Immunology, Weizmann Institute of Science, Rehovot, Israel.

European Journal of Immunology
|November 22, 1997
PubMed
Summary

Mast cell function-associated antigen (MAFA) is a glycoprotein that binds to mannose. This finding suggests MAFA

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Area of Science:

  • Immunology
  • Glycobiology
  • Cell Biology

Background:

  • Mast cell function-associated antigen (MAFA) is a membrane glycoprotein involved in regulating mast cell secretory responses.
  • MAFA was initially identified on rat mucosal mast cells (RBL-2H3) and is known to inhibit Fc epsilon RI-mediated secretion.
  • The extracellular domain of MAFA exhibits homology to carbohydrate-binding domains of calcium-dependent animal lectins.

Purpose of the Study:

  • To investigate the carbohydrate-binding capacity of MAFA.
  • To characterize the recombinant MAFA (rMAFA) expressed in insect cells.
  • To determine the specific saccharide ligands bound by rMAFA.

Main Methods:

  • Recombinant MAFA (rMAFA) was expressed in Spodoptera frugiperda (Sf9) insect cells using a baculovirus system.
  • Flow cytometry and 125I surface labeling were used to analyze rMAFA expression and characteristics.
  • Immunoaffinity-purified rMAFA was tested for saccharide binding using neoglycans and glycoproteins.

Main Results:

  • rMAFA was expressed as monomeric and disulfide-linked homodimeric glycoproteins on the insect cell membrane.
  • Both forms of rMAFA displayed epitopes identical to those of native MAFA from RBL-2H3 cells.
  • rMAFA specifically bound to terminal mannose residues in a calcium (Ca2+)-dependent manner.

Conclusions:

  • The extracellular domain of MAFA possesses functional carbohydrate-binding capabilities.
  • MAFA's ability to bind mannose suggests a role in modulating mast cell responses.
  • These findings provide insights into the molecular mechanisms of mast cell regulation.

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