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The Chicken Yolk Sac IgY Receptor, a Mammalian Mannose Receptor Family Member, Transcytoses IgY across Polarized Epithelial Cells

Tesar, Devin B. and Cheung, Evelyn J. and Bjorkman, Pamela J. (2008) The Chicken Yolk Sac IgY Receptor, a Mammalian Mannose Receptor Family Member, Transcytoses IgY across Polarized Epithelial Cells. Molecular Biology of the Cell, 19 (4). pp. 1587-1593. ISSN 1059-1524. PMCID PMC2291411. https://resolver.caltech.edu/CaltechAUTHORS:TESmbc08

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Abstract

In mammals the transfer of passive immunity from mother to young is mediated by the MHC-related receptor FcRn, which transports maternal IgG across epithelial cell barriers. In birds, maternal IgY in egg yolk is transferred across the yolk sac to passively immunize chicks during gestation and early independent life. The chicken yolk sac IgY receptor (FcRY) is the ortholog of the mammalian phospholipase A2 receptor, a mannose receptor family member, rather than an FcRn or MHC homolog. FcRn and FcRY both exhibit ligand binding at the acidic pH of endosomes and ligand release at the slightly basic pH of blood. Here we show that FcRY expressed in polarized mammalian epithelial cells functioned in endocytosis, bidirectional transcytosis, and recycling of chicken FcY/IgY. Confocal immunofluorescence studies demonstrated that IgY binding and endocytosis occurred at acidic but not basic pH, mimicking pH-dependent uptake of IgG by FcRn. Colocalization studies showed FcRY-mediated internalization via clathrin-coated pits and transport involving early and recycling endosomes. Disruption of microtubules partially inhibited apical-to-basolateral and basolateral-to-apical transcytosis, but not recycling, suggesting the use of different trafficking machinery. Our results represent the first cell biological evidence of functional equivalence between FcRY and FcRn and provide an intriguing example of how evolution can give rise to systems in which similar biological requirements in different species are satisfied utilizing distinct protein folds.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2291411/PubMed CentralArticle
https://doi.org/10.1091/mbc.E07-09-0972DOIUNSPECIFIED
https://doi.org/10.1091/mbc.E07-09-0972DOIUNSPECIFIED
ORCID:
AuthorORCID
Bjorkman, Pamela J.0000-0002-2277-3990
Additional Information:Copyright © 2008 by The American Society for Cell Biology. Under the License and Publishing Agreement, authors grant to the general public, effective two months after publication of (i.e.,. the appearance of) the edited manuscript in an online issue of MBoC, the nonexclusive right to copy, distribute, or display the manuscript subject to the terms of the Creative Commons–Noncommercial–Share Alike 3.0 Unported license (http://creativecommons.org/licenses/by-nc-sa/3.0). Submitted on September 27, 2007. Revised on January 4, 2008. Accepted on January 30, 2008. MBC in Press, published online ahead of print February 6, 2008. We thank Anthony West for construction of expression vectors; the Caltech Protein Expression Center for baculovirus expression of FcRY; and members of the Bjorkman Lab for critical reading of the manuscript. This work was supported by the National Institutes of Health (2 R37 AI041239-06A1 to P.J.B.)
Funders:
Funding AgencyGrant Number
NIH2 R37 AI041239-06A1
Issue or Number:4
PubMed Central ID:PMC2291411
Record Number:CaltechAUTHORS:TESmbc08
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:TESmbc08
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:9624
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:19 Feb 2008
Last Modified:03 Oct 2019 00:02

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