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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2020
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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. |
format | Online Article Text |
id | pubmed-7244179 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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