Opsonin-independent ligation of Fc gamma receptors. The 3G8-bearing receptors on neutrophils mediate the phagocytosis of concanavalin A-treated erythrocytes and nonopsonized Escherichia coli. Academic Article uri icon

Overview

abstract

  • We report that phagocytosis by human neutrophils of Con A-treated erythrocytes (E-Con A) and nonopsonized Escherichia coli with mannose-binding adhesions is mediated by the Fc gamma receptor bearing the 3G8 epitope. Modulation of Fc receptors by pretreating with aggregated-IgG or with 3G8 anti-Fc gamma receptor mAb markedly inhibited internalization of E-Con A and E. coli without altering their cell surface attachment. Phagocytosis of these probes was specifically blocked by alpha-methylmannoside and D-mannose and not by other monosaccharides. Thus, recognition of E-Con A and E. coli by the Fc receptor is dependent upon the mannose-specific interaction with lectin or lectin-like adhesions. These data demonstrate that ligands other than the classical IgG opsonins can bind to classical immune receptors for IgG through lectin-carbohydrate interactions.

publication date

  • December 1, 1987

Research

keywords

  • Glycoproteins
  • Membrane Glycoproteins
  • Neutrophils
  • Opsonin Proteins
  • Phagocytosis
  • Receptors, Fc

Identity

PubMed Central ID

  • PMC2188782

Scopus Document Identifier

  • 0023491107

Digital Object Identifier (DOI)

  • 10.1084/jem.166.6.1798

PubMed ID

  • 2445895

Additional Document Info

volume

  • 166

issue

  • 6