We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Cell surface expression of a human IgC Fc chimera activates macrophages through Fc receptors.
- Authors
Stabila, Paul F.; Wong, Shou C.; Kaplan, Faith A.; Tao, Weng
- Abstract
Antibody-dependent cell-mediated cytotoxicity plays an important role in the macrophage-mediated destruction of target cells. While the selectivity is based on antibody specificity, the lytic attack is triggered by Fc receptor-mediated respiratory burst. To mimic IgG opsonization, a chimeric antibody-like molecule, containing human IgG1 Fc, was expressed on the surface of mammalian cells. The transmem-brane domain of the human transferrin receptor was fused in-frame to the N-terminus of the second and third domains of human IgG1 heavy-chain constant region. This fusion molecule was designed to take advantage of the type II membrane anchor property of the transferrin receptor to express the Fc portion of the molecule in a reverse orientation, such that the Fc portion projected away from the cell surface. This is in contrast to the conventional cell surface IgG, which is anchored by a C-terminal type I trans-membrane domain. The cell surface expressed reverse Fc no longer activated complement, but retained Fc receptor-binding capability and activated superoxide production by macrophages. This activity was completely blocked by an Fc&gama;R I-specific monoclonal antibody.
- Subjects
IMMUNOGLOBULIN G; CELL-mediated cytotoxicity
- Publication
Nature Biotechnology, 1998, Vol 16, Issue 13, p1357
- ISSN
1087-0156
- Publication type
Article
- DOI
10.1038/4339