Bacterial glycosidases for the production of universal red blood cells
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/665895
- author
- Liu, Qiyong P.
; Sulzenbacher, Gerlind
; Yuan, Huaiping
; Bennett, Eric P.
; Pietz, Greg
; Saunders, Kristen
; Spence, Jean
; Nudelman, Edward
; Levery, Steven B.
; White, Thayer
; Neveu, John M.
; Lane, William S.
; Bourne, Yves
; Olsson, Martin L
LU
; Henrissat, Bernard
and Clausen, Henrik
(Less) - organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- in
- 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
- LU publication?
- yes
- id
- 7eacb205-e738-4bf1-a5d0-4a9bdcf2e518 (old id 665895)
- date added to LUP
- 2016-04-01 16:30:12
- date last changed
- 2024-10-26 22:24:09
@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}},
doi = {{10.1038/nbt1298}},
volume = {{25}},
year = {{2007}},
}