Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O

Kruskall, Margot S.; AuBuchon, James P.; Anthony, Kathleen Y.; Herschel, Louise; Pickard, Connie; Biehl, Ruth; Horowitz, Marilyn S.; Brambilla, Donald; Popovsky, Mark

doi:10.1046/j.1537-2995.2000.40111290.x

Cited by 61 publications

(37 citation statements)

References 27 publications

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“…54 In a more biomedical context, GLA has application in blood transfusion by removing the immunodominant a-1,3-linked galactose residues from group B red blood cells. 55,56 Enzymatic conversion of group B red blood cells using purified or recombinant coffee bean GLA has been achieved, 57,58 but the high amounts of enzyme needed constituted an economic obstacle for routine use in blood transfusions.…”

Section: Discussionmentioning

confidence: 99%

Integrated approach to produce a recombinant, his‐tagged human α‐galactosidase a in mammalian cells

Corchero

Mendoza

Lorenzo

et al. 2011

Biotechnology Progress

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Successful production of recombinant proteins (r-proteins) by transient gene expression (TGE) depends on several parameters (including producer cells, culture conditions, transfection procedure, or expression vector) that should be optimized when producing any recombinant product. In this work, TGE-based production of human α-galactosidase A (GLA) is described. Producer cells, expression vectors, and parameters influencing cell metabolism after transfection have been tested. The enzyme is secreted, has the right molecular weight, and is enzymatically active. Productivities of up to 30-40 mg/L have been achieved, with a simple, fast procedure. A 6 × His tag allows enzyme purification in a single step, rendering a highly pure product. We propose a TGE-based protocol able to produce up to several milligrams per liter of highly pure, active GLA in a time as short as a few days. By this, enough amounts of engineered versions of the enzyme can be easily produced to be tested in vitro or in preclinical trials.

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Section: Discussionmentioning

confidence: 99%

Integrated approach to produce a recombinant, his‐tagged human α‐galactosidase a in mammalian cells

Corchero

Mendoza

Lorenzo

et al. 2011

Biotechnology Progress

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“…This is confirmed by biochemical results (Liu et al, 2007) which verify that A and B antigens carried by both glycoproteins and glycolipids closer to the membrane are effectively digested, even if trace amounts can be detected with extremely sensitive methodology. These data are promising in the light of B-ECO RBCs generated with the older coffee bean process which survived and recovered normally in group O subjects (Kruskall et al, 2000) despite carrying minimal levels of remaining B antigen.…”

Section: Development Of the Eco Process And Characterization Of The Ementioning

confidence: 84%

“…A successful phase II cross-over clinical trial in patients was reported in 2000 (Kruskall et al, 2000). (Kruskall et al, 2000). The cross-match results obtained with the new A-ECO and B-ECO RBCs are similar and positive reactions can be found, mainly with group O sera and to a lesser extent with group B.…”

Section: Clinical Experience With Eco Rbcsmentioning

confidence: 95%

“…Despite this, coffee-bean-derived enzyme was successfully used to complete phase I (Lenny et al, 1991(Lenny et al, , 1994(Lenny et al, , 1995 and phase II clinical trials in which B-ECO RBCs were shown to be safe and functional, providing RBC survival and recovery values equal to ABO-compatible control transfusions in patients during a randomized cross-over study (Kruskall et al, 2000).…”

Section: The Eco Process and The Enzymesmentioning

confidence: 99%

“…Clinical phase I studies were conducted using B-ECO RBCs given to group A and O healthy volunteers and the initial small infusions were escalated to full single RBC units (Lenny et al, 1991), multiple units and finally repeated transfusions (Lenny et al, 1994(Lenny et al, , 1995. A successful phase II cross-over clinical trial in patients was reported in 2000 (Kruskall et al, 2000). (Kruskall et al, 2000).…”

Section: Clinical Experience With Eco Rbcsmentioning

confidence: 99%

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Modifying the red cell surface: towards an ABO‐universal blood supply

Olsson¹,

Clausen²

2007

Br J Haematol

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SummaryEliminating the risk for ABO-incompatible transfusion errors and simplifying logistics by creating a universal blood inventory is a challenging idea. Goldstein and co-workers pioneered the field of enzymatic conversion of blood group A and B red blood cells (RBCs) to O (ECO). Using a-galactosidase from coffee beans to produce B-ECO RBCs, proof of principle for this revolutionary concept was achieved in clinical trials. However, because this enzyme has poor kinetic properties and low pH optimum the process was not economically viable. Conversion of group A RBCs was only achieved with the weak A 2 subgroup with related enzymes having acidic pH optima. More recently, the identification of entirely new families of bacterial exoglycosidases with remarkably improved kinetic properties for cleaving A and B antigens has reinvigorated the field. Enzymatic conversion of groups A, B and AB RBCs with these novel enzymes resulting in ECO RBCs typing as O can now be achieved with low enzyme protein consumption, short incubation times and at neutral pH. Presently, clinical trials evaluating safety and efficacy of ECO RBCs are ongoing. Here, we review the status of the ECO technology, its impact and potential for introduction into clinical component preparation laboratories.

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ABO, Lewis and P Groups and Ii Antigens

Klein¹,

Anstee²

2005

Mollison's Blood Transfusion in Clinical Medicine

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Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O

Cited by 61 publications

References 27 publications

Integrated approach to produce a recombinant, his‐tagged human α‐galactosidase a in mammalian cells

Integrated approach to produce a recombinant, his‐tagged human α‐galactosidase a in mammalian cells

Modifying the red cell surface: towards an ABO‐universal blood supply

ABO, Lewis and P Groups and Ii Antigens

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