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Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII

Human coagulation factor VIII (FVIII) is a key co-factor in the clotting cascade, the deficiency of which leads to Hemophilia A. Human plasma-derived (pdFVIII) and recombinant FVIII (rFVIII) had been used as effective products to prevent and treat bleeding episodes. Both FVIII products share identic...

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Autores principales: Qu, Jingyao, Ma, Cheng, Xu, Xiao-Qian, Xiao, Min, Zhang, Junping, Li, Dong, Liu, Ding, Konkle, Barbara A., Miao, Carol H., Li, Lei, Xiao, Weidong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7244179/
https://www.ncbi.nlm.nih.gov/pubmed/32442215
http://dx.doi.org/10.1371/journal.pone.0233576
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author Qu, Jingyao
Ma, Cheng
Xu, Xiao-Qian
Xiao, Min
Zhang, Junping
Li, Dong
Liu, Ding
Konkle, Barbara A.
Miao, Carol H.
Li, Lei
Xiao, Weidong
author_facet Qu, Jingyao
Ma, Cheng
Xu, Xiao-Qian
Xiao, Min
Zhang, Junping
Li, Dong
Liu, Ding
Konkle, Barbara A.
Miao, Carol H.
Li, Lei
Xiao, Weidong
author_sort Qu, Jingyao
collection PubMed
description Human coagulation factor VIII (FVIII) is a key co-factor in the clotting cascade, the deficiency of which leads to Hemophilia A. Human plasma-derived (pdFVIII) and recombinant FVIII (rFVIII) had been used as effective products to prevent and treat bleeding episodes. Both FVIII products share identical amino acid sequences and appear to be equivalent as of clinical efficiency. However, systemic reviews found an increased risk of neutralizing antibody (or inhibitor) development with recombinant products. FVIII is a highly glycosylated protein, and its glycosylation pattern is specific to host cells and environments. The roles of glycosylation in immune responses toward pdFVIII and rFVIII are yet to be defined. Herein, we systemically profiled N- and O-glycomes of pdFVIII and rFVIII using a mass spectrometry-based glycoproteomic strategy. A total of 110 site-specific N-glycopeptides consisting of 61 N-glycoforms were identified quantitatively from rFVIII and pdFVIII. Additionally, 31 O-glycoforms were identified on 23 peptides from rFVIII and pdFVIII. A comprehensive comparison of their site-specific glycan profiles revealed distinct differences between the glycosylation of pdFVIII and rFVIII.
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spelling pubmed-72441792020-06-05 Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII Qu, Jingyao Ma, Cheng Xu, Xiao-Qian Xiao, Min Zhang, Junping Li, Dong Liu, Ding Konkle, Barbara A. Miao, Carol H. Li, Lei Xiao, Weidong PLoS One Research Article Human coagulation factor VIII (FVIII) is a key co-factor in the clotting cascade, the deficiency of which leads to Hemophilia A. Human plasma-derived (pdFVIII) and recombinant FVIII (rFVIII) had been used as effective products to prevent and treat bleeding episodes. Both FVIII products share identical amino acid sequences and appear to be equivalent as of clinical efficiency. However, systemic reviews found an increased risk of neutralizing antibody (or inhibitor) development with recombinant products. FVIII is a highly glycosylated protein, and its glycosylation pattern is specific to host cells and environments. The roles of glycosylation in immune responses toward pdFVIII and rFVIII are yet to be defined. Herein, we systemically profiled N- and O-glycomes of pdFVIII and rFVIII using a mass spectrometry-based glycoproteomic strategy. A total of 110 site-specific N-glycopeptides consisting of 61 N-glycoforms were identified quantitatively from rFVIII and pdFVIII. Additionally, 31 O-glycoforms were identified on 23 peptides from rFVIII and pdFVIII. A comprehensive comparison of their site-specific glycan profiles revealed distinct differences between the glycosylation of pdFVIII and rFVIII. Public Library of Science 2020-05-22 /pmc/articles/PMC7244179/ /pubmed/32442215 http://dx.doi.org/10.1371/journal.pone.0233576 Text en © 2020 Qu et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Qu, Jingyao
Ma, Cheng
Xu, Xiao-Qian
Xiao, Min
Zhang, Junping
Li, Dong
Liu, Ding
Konkle, Barbara A.
Miao, Carol H.
Li, Lei
Xiao, Weidong
Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII
title Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII
title_full Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII
title_fullStr Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII
title_full_unstemmed Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII
title_short Comparative glycosylation mapping of plasma-derived and recombinant human factor VIII
title_sort comparative glycosylation mapping of plasma-derived and recombinant human factor viii
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7244179/
https://www.ncbi.nlm.nih.gov/pubmed/32442215
http://dx.doi.org/10.1371/journal.pone.0233576
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