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An Fc receptor structurally related to MHC class I antigens

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Abstract

Maternal immunoglobulin G transmitted to the fetus or newborn provides humoral immunity for the first weeks of mammalian life. Fc receptors on intestinal epithelial cells of the neonatal rat (FcRn) mediate the uptake of IgG from milk. Affinity-purified FcRn is resolved by SDS-PAGE into components of relative molecular masses 45,000–53,000 (p51) and about 14,000 (p14)1–3. We report the identification of the smaller component as β2-microglobulin. Association of β2-microglobulin with p51 was confirmed by cross-linking in intestinal epithelial cell brush borders. We have cloned a cDNA encoding the presumptive Fc-binding subunit, p51, and its predicted primary structure has three extracellular domains and a transmembrane region which are all homologous to the corresponding domains of class I major histocompatibility complex (MHC) antigens. This is the first time a function has been assigned to an MHC antigen-related molecule.

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Authors and Affiliations

  1. Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, Massachusetts, 02142, USA

    Neil E. Simister & Keith E. Mostov

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  1. Neil E. Simister
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  2. Keith E. Mostov
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Simister, N., Mostov, K. An Fc receptor structurally related to MHC class I antigens. Nature 337, 184–187 (1989). https://doi.org/10.1038/337184a0

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