The University of Southampton
University of Southampton Institutional Repository

Localization of the site of the IgG molecule that regulates maternofetal transmission in mice

Localization of the site of the IgG molecule that regulates maternofetal transmission in mice
Localization of the site of the IgG molecule that regulates maternofetal transmission in mice

Site-directed mutagenesis of a recombinant Fc hinge fragment has recently been used to localize the site of the mouse IgG1 (mIgG1) molecule that is involved in the intestinal transfer of recombinant Fc hinge fragments in neonatal mice. This site encompasses Ile-253, His-310, Gln-311, His-433 and Asn-434, localized at the CH2-CH3 domain interface and overlapping with the staphylococcal protein A-binding and catabolic sites. In the present study, the effect of these mutations on the maternofetal transfer of Fc hinge fragments has been studied. Experiments to analyze transfer of radiolabeled Fc hinge fragments from the circulation of 15-18 day pregnant mice to fetuses in utero demonstrate that the mutations affect the maternofetal transmission in a way that correlates closely with the effects of the mutations on intestinal transfer and catabolism. The studies indicate that the neonatal Fc receptor, FcRn, is involved in transcytosis across both yolk sac and neonatal intestine in addition to the regulation of IgG catabolism.

IgG, Maternofetal transmission, Neonatal Fc receptor
0014-2980
2533-2536
Medesan, Comeliu
0de1d9e4-c8d9-4896-bcca-63f8b24e8f2c
Radu, Caius
7b0cdea8-4ad8-4c89-89f7-eb6083504c1c
Kim, Jin Kyoo
3f679975-b86c-4b96-9571-499c2ad80378
Ghetie, Victor
b7b50946-2bd9-4896-b841-6bbfba8237c2
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc
Medesan, Comeliu
0de1d9e4-c8d9-4896-bcca-63f8b24e8f2c
Radu, Caius
7b0cdea8-4ad8-4c89-89f7-eb6083504c1c
Kim, Jin Kyoo
3f679975-b86c-4b96-9571-499c2ad80378
Ghetie, Victor
b7b50946-2bd9-4896-b841-6bbfba8237c2
Ward, E. Sally
b31c0877-8abe-485f-b800-244a9d3cd6cc

Medesan, Comeliu, Radu, Caius, Kim, Jin Kyoo, Ghetie, Victor and Ward, E. Sally (1996) Localization of the site of the IgG molecule that regulates maternofetal transmission in mice. European Journal of Immunology, 26 (10), 2533-2536. (doi:10.1002/eji.1830261038).

Record type: Article

Abstract

Site-directed mutagenesis of a recombinant Fc hinge fragment has recently been used to localize the site of the mouse IgG1 (mIgG1) molecule that is involved in the intestinal transfer of recombinant Fc hinge fragments in neonatal mice. This site encompasses Ile-253, His-310, Gln-311, His-433 and Asn-434, localized at the CH2-CH3 domain interface and overlapping with the staphylococcal protein A-binding and catabolic sites. In the present study, the effect of these mutations on the maternofetal transfer of Fc hinge fragments has been studied. Experiments to analyze transfer of radiolabeled Fc hinge fragments from the circulation of 15-18 day pregnant mice to fetuses in utero demonstrate that the mutations affect the maternofetal transmission in a way that correlates closely with the effects of the mutations on intestinal transfer and catabolism. The studies indicate that the neonatal Fc receptor, FcRn, is involved in transcytosis across both yolk sac and neonatal intestine in addition to the regulation of IgG catabolism.

This record has no associated files available for download.

More information

Accepted/In Press date: 16 July 1996
Published date: October 1996
Keywords: IgG, Maternofetal transmission, Neonatal Fc receptor

Identifiers

Local EPrints ID: 425115
URI: http://eprints.soton.ac.uk/id/eprint/425115
ISSN: 0014-2980
PURE UUID: f49c42f4-4fd9-4395-8541-1f27acf3cdab
ORCID for E. Sally Ward: ORCID iD orcid.org/0000-0003-3232-7238

Catalogue record

Date deposited: 11 Oct 2018 16:30
Last modified: 16 Mar 2024 04:37

Export record

Altmetrics

Contributors

Author: Comeliu Medesan
Author: Caius Radu
Author: Jin Kyoo Kim
Author: Victor Ghetie
Author: E. Sally Ward ORCID iD

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×