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dc.date.accessioned2017-03-07T16:18:58Z
dc.date.available2017-03-07T16:18:58Z
dc.date.created2006-08-31T10:02:01Z
dc.date.issued2006
dc.identifier.citationBraathen, Ranveig Sandvik, Anders Berntzen, Gøril Hammerschmidt, S Fleckenstein, Burkhard Sandlie, Inger Brandtzæg, Per Johansen, Finn Eirik Lauvrak, Vigdis . Identification of a polymeric Ig receptor binding phage-displayed peptide that exploits epithelial transcytosis without dimeric IgA competition. Journal of Biological Chemistry. 2006, 281, 7075-7081
dc.identifier.urihttp://hdl.handle.net/10852/54502
dc.description.abstractThe polymeric Ig receptor (pIgR), also called membrane secretory component (SC), mediates epithelial transcytosis of polymeric immunoglobulins (pIgs). J Chain-containing polymeric IgA (pIgA) and pentameric IgM bind pIgR at the basolateral epithelial surface. After transcytosis, the extracellular portion of the pIgR is cleaved at the apical side, either complexed with pIgs as bound SC or unoccupied as free SC. This transport pathway may be exploited to target bioactive molecules to the mucosal surface. To identify small peptide motifs with specific affinity to human pIgR, we used purified free SC and selection from randomized, cysteine-flanked 6- and 9-mer phage-display libraries. One of the selected phages, called C9A, displaying the peptide CVVWMGFQQVC, showed binding both to human free SC and SC complexed with pIgs. However, the pneumococcal surface protein SpsA (Streptococcus pneumoniae secretory IgA-binding protein), which binds human SC at a site distinct from the pIg binding site, competed with the C9A phage for binding to SC. The C9A phage showed greatly increased transport through polarized Madin-Darby canine kidney cells transfected with human pIgR. This transport was not affected by pIgA nor did it inhibit pIgR-mediated pIgA transcytosis. A free peptide of identical amino acid sequence as that displayed by the C9A phage inhibited phage interaction with SC. This implied that the C9A peptide sequence may be exploited for pIgR-mediated epithelial transport without interfering with secretory immunity. This research was originally published in: Journal of Biological Chemistry. © the American Society for Biochemistry and Molecular Biology.en_US
dc.languageEN
dc.titleIdentification of a polymeric Ig receptor binding phage-displayed peptide that exploits epithelial transcytosis without dimeric IgA competitionen_US
dc.typeJournal articleen_US
dc.creator.authorBraathen, Ranveig
dc.creator.authorSandvik, Anders
dc.creator.authorBerntzen, Gøril
dc.creator.authorHammerschmidt, S
dc.creator.authorFleckenstein, Burkhard
dc.creator.authorSandlie, Inger
dc.creator.authorBrandtzæg, Per
dc.creator.authorJohansen, Finn Eirik
dc.creator.authorLauvrak, Vigdis
cristin.unitcode185,13,14,6
cristin.unitnamePatologiklinikken
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2
dc.identifier.cristin379626
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal of Biological Chemistry&rft.volume=281&rft.spage=7075&rft.date=2006
dc.identifier.jtitleJournal of Biological Chemistry
dc.identifier.volume281
dc.identifier.startpage7075
dc.identifier.endpage7081
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M508509200
dc.identifier.urnURN:NBN:no-57625
dc.type.documentTidsskriftartikkelen_US
dc.type.peerreviewedPeer reviewed
dc.source.issn0021-9258
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/54502/1/56.%2BJ.%2BBiol.%2BChem.-2006-Braathen-7075-81.pdf
dc.type.versionPublishedVersion


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