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Sökning: WFRF:(Bergseth Grethe) > (2017) > Eculizumab-C5 compl...

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FältnamnIndikatorerMetadata
00003906naa a2200481 4500
001oai:DiVA.org:lnu-68145
003SwePub
008171002s2017 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-681452 URI
0247 a https://doi.org/10.1016/j.molimm.2017.05.0212 DOI
040 a (SwePub)lnu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Nilsson, Per H.,d 1980-u Linnéuniversitetet,Institutionen för kemi och biomedicin (KOB),Oslo Univ Hosp, Norway;Univ Oslo, Norway,Linnaeus Ctr Biomat Chem, BMC;HoRB4 aut0 (Swepub:lnu)enipe
2451 0a Eculizumab-C5 complexes express a C5a neoepitope in vivo :b Consequences for interpretation of patient complement analyses
264 1b Elsevier,c 2017
338 a electronic2 rdacarrier
520 a The complement system has obtained renewed clinical focus due to increasing number of patients treated with eculizumab, a monoclonal antibody inhibiting cleavage of C5 into C5a and C5b. The FDA approved indications are paroxysmal nocturnal haemoglobinuria and atypical haemolytic uremic syndrome, but many other diseases are candidates for complement inhibition. It has been postulated that eculizumab does not inhibit C5a formation in vivo, in contrast to what would be expected since it blocks C5 cleavage. We recently revealed that this finding was due to a false positive reaction in a C5a assay. In the present study, we identified expression of a neoepitope which was exposed on C5 after binding to eculizumab in vivo. By size exclusion chromatography of patient serum obtained before and after infusion of eculizumab, we document that the neoepitope was exposed in the fractions containing the eculizumab-C5 complexes, being positive in this actual C5a assay and negative in others. Furthermore, we confirmed that it was the eculizumab-C5 complexes that were detected in the C5a assay by adding an anti-IgG4 antibody as detection antibody. Competitive inhibition by anti-C5 antibodies localized the epitope to the C5a moiety of C5. Finally, acidification of C5, known to alter C5 conformation, induced a neoepitope reacting identical to the one we explored, in the C5a assays. These data are important for interpretation of complement analyses in patients treated with eculizumab.
650 7a NATURVETENSKAPx Biologix Immunologi0 (SwePub)106052 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Immunology0 (SwePub)106052 hsv//eng
653 a Complement
653 a Eculizumab
653 a C5
653 a C5a
653 a Neoepitope
653 a Immunologi
653 a Immunology
7001 a Thomas, Anub Mathewu Oslo Univ Hosp, Norway4 aut
7001 a Bergseth, Gretheu Nordland Hosp, Norway4 aut
7001 a Gustavsen, Aliceu Oslo Univ Hosp, Norway4 aut
7001 a Volokhina, Elena B.u Radboud Univ Nijmegen, Netherlands;Radboud Univ Nijmegen, Netherlands4 aut
7001 a van den Heuvel, Lambertus P.u Radboud Univ Nijmegen, Netherlands;Univ Hosp Leuven, Belgium4 aut
7001 a Barratt-Due, Andreasu Oslo Univ Hosp, Norway4 aut
7001 a Mollnes, Tom E.u Oslo Univ Hosp, Norway;Univ Oslo, Norway;Nordland Hosp, Norway;Univ Tromso, Norway;Norwegian Univ Sci & Technol, Norway4 aut
7102 a Linnéuniversitetetb Institutionen för kemi och biomedicin (KOB)4 org
7730 t Molecular Immunologyd : Elsevierg 89, s. 111-114q 89<111-114x 0161-5890x 1872-9142
8564 u https://doi.org/10.1016/j.molimm.2017.05.021y Fulltext
8564 u https://lnu.diva-portal.org/smash/get/diva2:1146254/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
8564 u https://doi.org/10.1016/j.molimm.2017.05.021
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-68145
8564 8u https://doi.org/10.1016/j.molimm.2017.05.021

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