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The Fc Domain of Immunoglobulin Is Sufficient to Bridge NK Cells with Virally Infected Cells.

Immunity | Jul 18, 2017

Clearance of pathogens or tumor cells by antibodies traditionally requires both Fab and Fc domains of IgG. Here, we show the Fc domain of IgG alone mediates recognition and clearance of herpes simplex virus (HSV1)-infected cells. The human natural killer (NK) cell surface is naturally coated with IgG bound by its Fc domain to the Fcγ receptor CD16a. NK cells utilize the Fc domain of bound IgG to recognize gE, an HSV1-encoded glycoprotein that also binds the Fc domain of IgG but at a site distinct from CD16a. The bridge formed by the Fc domain between the HSV1-infected cell and the NK cell results in NK cell activation and lysis of the HSV1-infected cell in the absence of HSV1-specific antibody in vitro and prevents fatal HSV1 infection in vivo. This mechanism also explains how bacterial IgG-binding proteins regulate NK cell function and may be broadly applicable to Fcγ-receptor-bearing cells.

Pubmed ID: 28723548 RIS Download

Mesh terms: Animals | Antibodies, Viral | Cells, Cultured | Cytotoxicity, Immunologic | Female | Herpes Simplex | Humans | Immunoglobulin Fc Fragments | Immunoglobulin G | Killer Cells, Natural | Lymphocyte Activation | Mice | Mice, Inbred BALB C | Mice, Inbred C57BL | Protein Binding | Receptor Aggregation | Receptors, IgG | Signal Transduction | Simplexvirus | Viral Proteins

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Associated grants

  • Agency: NCI NIH HHS, Id: R01 CA155521
  • Agency: NCI NIH HHS, Id: R35 CA210087
  • Agency: NCI NIH HHS, Id: P01 CA095426
  • Agency: NCI NIH HHS, Id: P30 CA016058
  • Agency: NCI NIH HHS, Id: P01 CA163205
  • Agency: NCI NIH HHS, Id: R37 CA068458

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