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Bacterial glycosidases for the production of universal red blood cells

Liu, Qiyong P.; Sulzenbacher, Gerlind; Yuan, Huaiping; Bennett, Eric P.; Pietz, Greg; Saunders, Kristen; Spence, Jean; Nudelman, Edward; Levery, Steven B. and White, Thayer, et al. (2007) In Nature Biotechnology 25(4). p.454-464
Abstract
Enzymatic removal of blood group ABO antigens to develop universal red blood cells ( RBCs) was a pioneering vision originally proposed more than 25 years ago. Although the feasibility of this approach was demonstrated in clinical trials for group B RBCs, a major obstacle in translating this technology to clinical practice has been the lack of efficient glycosidase enzymes. Here we report two bacterial glycosidase gene families that provide enzymes capable of efficient removal of A and B antigens at neutral pH with low consumption of recombinant enzymes. The crystal structure of a member of the alpha-N-acetylgalactosaminidase family reveals an unusual catalytic mechanism involving NAD(+). The enzymatic conversion processes we describe hold... (More)
Enzymatic removal of blood group ABO antigens to develop universal red blood cells ( RBCs) was a pioneering vision originally proposed more than 25 years ago. Although the feasibility of this approach was demonstrated in clinical trials for group B RBCs, a major obstacle in translating this technology to clinical practice has been the lack of efficient glycosidase enzymes. Here we report two bacterial glycosidase gene families that provide enzymes capable of efficient removal of A and B antigens at neutral pH with low consumption of recombinant enzymes. The crystal structure of a member of the alpha-N-acetylgalactosaminidase family reveals an unusual catalytic mechanism involving NAD(+). The enzymatic conversion processes we describe hold promise for achieving the goal of producing universal RBCs, which would improve the blood supply while enhancing the safety of clinical transfusions. (Less)
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publication status
published
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Nature Biotechnology
volume
25
issue
4
pages
454 - 464
publisher
Nature Publishing Group
external identifiers
  • wos:000245651800027
  • scopus:34147142476
ISSN
1546-1696
DOI
10.1038/nbt1298
language
English
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yes
id
7eacb205-e738-4bf1-a5d0-4a9bdcf2e518 (old id 665895)
date added to LUP
2007-12-17 09:00:56
date last changed
2017-10-09 09:43:29
@article{7eacb205-e738-4bf1-a5d0-4a9bdcf2e518,
  abstract     = {Enzymatic removal of blood group ABO antigens to develop universal red blood cells ( RBCs) was a pioneering vision originally proposed more than 25 years ago. Although the feasibility of this approach was demonstrated in clinical trials for group B RBCs, a major obstacle in translating this technology to clinical practice has been the lack of efficient glycosidase enzymes. Here we report two bacterial glycosidase gene families that provide enzymes capable of efficient removal of A and B antigens at neutral pH with low consumption of recombinant enzymes. The crystal structure of a member of the alpha-N-acetylgalactosaminidase family reveals an unusual catalytic mechanism involving NAD(+). The enzymatic conversion processes we describe hold promise for achieving the goal of producing universal RBCs, which would improve the blood supply while enhancing the safety of clinical transfusions.},
  author       = {Liu, Qiyong P. and Sulzenbacher, Gerlind and Yuan, Huaiping and Bennett, Eric P. and Pietz, Greg and Saunders, Kristen and Spence, Jean and Nudelman, Edward and Levery, Steven B. and White, Thayer and Neveu, John M. and Lane, William S. and Bourne, Yves and Olsson, Martin L and Henrissat, Bernard and Clausen, Henrik},
  issn         = {1546-1696},
  language     = {eng},
  number       = {4},
  pages        = {454--464},
  publisher    = {Nature Publishing Group},
  series       = {Nature Biotechnology},
  title        = {Bacterial glycosidases for the production of universal red blood cells},
  url          = {http://dx.doi.org/10.1038/nbt1298},
  volume       = {25},
  year         = {2007},
}