Please use this identifier to cite or link to this item: https://doi.org/10.1038/nature07255
DC FieldValue
dc.titleFcRn-mediated antibody transport across epithelial cells revealed by electron tomography
dc.contributor.authorHe, W.
dc.contributor.authorLadinsky, M.S.
dc.contributor.authorHuey-Tubman, K.E.
dc.contributor.authorJensen, G.J.
dc.contributor.authorMcIntosh, J.R.
dc.contributor.authorBjörkman, P.J.
dc.date.accessioned2014-10-27T08:28:23Z
dc.date.available2014-10-27T08:28:23Z
dc.date.issued2008-09-25
dc.identifier.citationHe, W., Ladinsky, M.S., Huey-Tubman, K.E., Jensen, G.J., McIntosh, J.R., Björkman, P.J. (2008-09-25). FcRn-mediated antibody transport across epithelial cells revealed by electron tomography. Nature 455 (7212) : 542-546. ScholarBank@NUS Repository. https://doi.org/10.1038/nature07255
dc.identifier.issn00280836
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100668
dc.description.abstractThe neonatal Fc receptor (FcRn) transports maternal IgG across epithelial barriers, thereby providing the fetus or newborn with humoral immunity before its immune system is fully functional. In newborn rats, FcRn transfers IgG from milk to blood by apical-to-basolateral transcytosis across intestinal epithelial cells. The pH difference between the apical (pH 6.0-6.5) and basolateral (pH 7.4) sides of intestinal epithelial cells facilitates the efficient unidirectional transport of IgG, because FcRn binds IgG at pH 6.0-6.5 but not at pH 7 or more. As milk passes through the neonatal intestine, maternal IgG is removed by FcRn-expressing cells in the proximal small intestine (duodenum and jejunum); remaining proteins are absorbed and degraded by FcRn-negative cells in the distal small intestine (ileum). Here we use electron tomography to make jejunal transcytosis visible directly in space and time, developing new labelling and detection methods to map individual nanogold-labelled Fc within transport vesicles and simultaneously to characterize these vesicles by immunolabelling. Combining electron tomography with a non-perturbing endocytic label allowed us to conclusively identify receptor-bound ligands, resolve interconnecting vesicles, determine whether a vesicle was microtubule- associated, and accurately trace FcRn-mediated transport of IgG. Our results present a complex picture in which Fc moves through networks of entangled tubular and irregular vesicles, only some of which are microtubule-associated, as it migrates to the basolateral surface. New features of transcytosis are elucidated, including transport involving multivesicular body inner vesicles/tubules and exocytosis through clathrin-coated pits. Markers for early, late and recycling endosomes each labelled vesicles in different and overlapping morphological classes, revealing spatial complexity in endo-lysosomal trafficking. ©2008 Macmillan Publishers Limited. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/nature07255
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1038/nature07255
dc.description.sourcetitleNature
dc.description.volume455
dc.description.issue7212
dc.description.page542-546
dc.description.codenNATUA
dc.identifier.isiut000259449600048
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

127
checked on May 17, 2022

WEB OF SCIENCETM
Citations

116
checked on May 17, 2022

Page view(s)

108
checked on May 12, 2022

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.